|
Name |
Accession |
Description |
Interval |
E-value |
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-331 |
0e+00 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 633.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 1 MALLDICNLNIEIQTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKENWIITADRFRFHDVELLKLSP 80
Cdd:COG4170 1 MPLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTADRFRWNGIDLLKLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 81 HKRRKIVGKEISMIFQNPLSCLDPSRKIGKQLIQNIPNWTFKNKWWKWFGWKKRRAIELLHRVGIKDHRDIMASYPNELT 160
Cdd:COG4170 81 RERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAIPSWTFKGKWWQRFKWRKKRAIELLHRVGIKDHKDIMNSYPHELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 161 EGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCGQNTES 240
Cdd:COG4170 161 EGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVES 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 241 APTEILIESPHHPYTQALINAVPDFTQPLGFKTKLGTLEGTVPILEQMPIGCRLGPRCPFAQKKCMEKPRRLKIKQHEFS 320
Cdd:COG4170 241 GPTEQILKSPHHPYTKALLRSMPDFRQPLPHKSRLNTLPGSIPPLQHLPIGCRLGPRCPYAQKKCVETPRLRKIKGHEFA 320
|
330
....*....|.
gi 1403710885 321 CHYPINLREKN 331
Cdd:COG4170 321 CHFPLNMEEKK 331
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-330 |
0e+00 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 518.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 1 MALLDICNLNIEIQTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKENWIITADRFRFHDVELLKLSP 80
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 81 HKRRKIVGKEISMIFQNPLSCLDPSRKIGKQLIQNIPNWTFKNKWWKWFGWKKRRAIELLHRVGIKDHRDIMASYPNELT 160
Cdd:PRK15093 81 RERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIPGWTYKGRWWQRFGWRKRRAIELLHRVGIKDHKDAMRSFPYELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 161 EGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCGQNTES 240
Cdd:PRK15093 161 EGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVET 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 241 APTEILIESPHHPYTQALINAVPDFTQPLGFKTKLGTLEGTVPILEQMPIGCRLGPRCPFAQKKCMEKPRRLKIKQHEFS 320
Cdd:PRK15093 241 APSKELVTTPHHPYTQALIRAIPDFGSAMPHKSRLNTLPGAIPLLEHLPIGCRLGPRCPYAQRECIETPRLTGAKNHLYA 320
|
330
....*....|
gi 1403710885 321 CHYPINLREK 330
Cdd:PRK15093 321 CHFPLNMEEE 330
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-324 |
3.97e-111 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 326.24 E-value: 3.97e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 3 LLDICNLNIEIQTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKENwIITADRFRFHDVELLKLSPHK 82
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPP-GITSGEILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 83 RRKIVGKEISMIFQNPLSCLDPSRKIGKQLIQnipnwTFKNKWWKWFGWKKRRAIELLHRVGIKDHRDIMASYPNELTEG 162
Cdd:COG0444 80 LRKIRGREIQMIFQDPMTSLNPVMTVGDQIAE-----PLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 163 EGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCGQNTESAP 242
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 243 TEILIESPHHPYTQALINAVPDFTQPlgfKTKLGTLEGTVPILEQMPIGCRLGPRCPFAQKKCMEK-PRRLKIKQ-HEFS 320
Cdd:COG0444 235 VEELFENPRHPYTRALLSSIPRLDPD---GRRLIPIPGEPPSLLNPPSGCRFHPRCPYAMDRCREEePPLREVGPgHRVA 311
|
....
gi 1403710885 321 CHYP 324
Cdd:COG0444 312 CHLY 315
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-326 |
3.92e-85 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 260.44 E-value: 3.92e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 1 MALLDICNLNIEIQTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKENWIITADRFRFHDVELLKLSP 80
Cdd:PRK11022 1 MALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 81 HKRRKIVGKEISMIFQNPLSCLDPSRKIGKQLIQNIpnwtfKNKWWKWFGWKKRRAIELLHRVGIKDHRDIMASYPNELT 160
Cdd:PRK11022 81 KERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAI-----KVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 161 EGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCGQNTES 240
Cdd:PRK11022 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVET 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 241 APTEILIESPHHPYTQALINAVPDFTQPlgfKTKLGTLEGTVPILEQMPIGCRLGPRCPFAQKKC-MEKPRRLKIKQHEF 319
Cdd:PRK11022 236 GKAHDIFRAPRHPYTQALLRALPEFAQD---KARLASLPGVVPGKYDRPNGCLLNPRCPYATDRCrAEEPALNMLAGRQS 312
|
....*..
gi 1403710885 320 SCHYPIN 326
Cdd:PRK11022 313 KCHYPLD 319
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-268 |
1.10e-77 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 247.68 E-value: 1.10e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 1 MALLDICNLNIEIQTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKENWIITADRFRFHDVELLKLSP 80
Cdd:COG4172 4 MPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 81 HKRRKIVGKEISMIFQNPLSCLDPSRKIGKQLIQnipnwTFKNKWWKWFGWKKRRAIELLHRVGIKDHRDIMASYPNELT 160
Cdd:COG4172 84 RELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAE-----VLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 161 EGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCGQNTES 240
Cdd:COG4172 159 GGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQ 238
|
250 260
....*....|....*....|....*...
gi 1403710885 241 APTEILIESPHHPYTQALINAVPDFTQP 268
Cdd:COG4172 239 GPTAELFAAPQHPYTRKLLAAEPRGDPR 266
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-241 |
5.71e-71 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 220.46 E-value: 5.71e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 3 LLDICNLNIEIQTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKenwiITADRFRFHDVELLKLSPhK 82
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLK----PTSGSIIFDGKDLLKLSR-R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 83 RRKIVGKEISMIFQNPLSCLDPSRKIGKQLIQNIPNWTfknkwwKWFGWKKRRAIELLHRVGIKDHRDIMASYPNELTEG 162
Cdd:cd03257 76 LRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHG------KLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1403710885 163 EGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCGQNTESA 241
Cdd:cd03257 150 QRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-309 |
1.27e-69 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 220.75 E-value: 1.27e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 1 MALLDICNLNIEIQTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKENWIITADRfRFHDVELLKLSP 80
Cdd:PRK09473 10 DALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSA-TFNGREILNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 81 HKRRKIVGKEISMIFQNPLSCLDPSRKIGKQLIQnipnwTFKNKWWKWFGWKKRRAIELLHRVGIKDHRDIMASYPNELT 160
Cdd:PRK09473 89 KELNKLRAEQISMIFQDPMTSLNPYMRVGEQLME-----VLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 161 EGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCGQNTES 240
Cdd:PRK09473 164 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEY 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1403710885 241 APTEILIESPHHPYTQALINAVPDFTqplGFKTKLGTLEGTVPILEQMPIGCRLGPRCPFAQKKCMEKP 309
Cdd:PRK09473 244 GNARDVFYQPSHPYSIGLLNAVPRLD---AEGESLLTIPGNPPNLLRLPKGCPFQPRCPHAMEICSSAP 309
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
18-263 |
4.54e-63 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 208.99 E-value: 4.54e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 18 GRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKenwiITADRFRFHDVELLKLSPHKRRKIvGKEISMIFQN 97
Cdd:COG1123 276 GGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR----PTSGSILFDGKDLTKLSRRSLREL-RRRVQMVFQD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 98 PLSCLDPSRKIGKQL-----IQNIPNwtfknkwwkwFGWKKRRAIELLHRVGIKdhRDIMASYPNELTEGEGQKVMIAMA 172
Cdd:COG1123 351 PYSSLNPRMTVGDIIaeplrLHGLLS----------RAERRERVAELLERVGLP--PDLADRYPHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 173 VANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCGQNTESAPTEILIESPHH 252
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQH 498
|
250
....*....|.
gi 1403710885 253 PYTQALINAVP 263
Cdd:COG1123 499 PYTRALLAAVP 509
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-286 |
1.50e-61 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 205.14 E-value: 1.50e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 2 ALLDICNLNIeiQTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKENWIITaDRFRFHDVELLKLSPH 81
Cdd:COG1123 3 PLLEVRDLSV--RYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRIS-GEVLLDGRDLLELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 82 KRrkivGKEISMIFQNPLSCLDPSRkIGKQLIQNIPNwtfknkWWKWFGWKKRRAIELLHRVGIKDHRDimaSYPNELTE 161
Cdd:COG1123 80 LR----GRRIGMVFQDPMTQLNPVT-VGDQIAEALEN------LGLSRAEARARVLELLEAVGLERRLD---RYPHQLSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 162 GEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCGQNTESA 241
Cdd:COG1123 146 GQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDG 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1403710885 242 PTEILIESPhhpytQALiNAVPDFTQPLGFKTKlgTLEGTVPILE 286
Cdd:COG1123 226 PPEEILAAP-----QAL-AAVPRLGAARGRAAP--AAAAAEPLLE 262
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
18-324 |
1.27e-58 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 192.25 E-value: 1.27e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 18 GRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKenwiITADRFRFHDVELLKLSPHKRRKiVGKEISMIFQN 97
Cdd:COG4608 29 GVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEE----PTSGEILFDGQDITGLSGRELRP-LRRRMQMVFQD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 98 PLSCLDPSRKIGKQL-----IQNIpnwtfknkwwKWFGWKKRRAIELLHRVGIK-DHRDimaSYPNELTEGEGQKVMIAM 171
Cdd:COG4608 104 PYASLNPRMTVGDIIaeplrIHGL----------ASKAERRERVAELLELVGLRpEHAD---RYPHEFSGGQRQRIGIAR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 172 AVANQPRLLIADEPTNALE-STTAlQVFRLLSSMNQNQGTTILLTSND---IKSISewcDQISVLYCGQNTESAPTEILI 247
Cdd:COG4608 171 ALALNPKLIVCDEPVSALDvSIQA-QVLNLLEDLQDELGLTYLFISHDlsvVRHIS---DRVAVMYLGKIVEIAPRDELY 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1403710885 248 ESPHHPYTQALINAVPDfTQPLGFKTKLgTLEGTVPILEQMPIGCRLGPRCPFAQKKCMEKPRRLKIK--QHEFSCHYP 324
Cdd:COG4608 247 ARPLHPYTQALLSAVPV-PDPERRRERI-VLEGDVPSPLNPPSGCRFHTRCPYAQDRCATEEPPLREVgpGHQVACHLA 323
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-265 |
1.51e-57 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 186.93 E-value: 1.51e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 3 LLDICNLNIEIQTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKEnwiiTADRFRFHDVELlklsPHK 82
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERP----WSGEVTFDGRPV----TRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 83 RRKIVGKEISMIFQNPLSCLDPSRKIGKQL-----IQNIPNwtfknkwwkwfgwKKRRAIELLHRVGIkdHRDIMASYPN 157
Cdd:COG1124 73 RRKAFRRRVQMVFQDPYASLHPRHTVDRILaeplrIHGLPD-------------REERIAELLEQVGL--PPSFLDRYPH 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 158 ELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCGQN 237
Cdd:COG1124 138 QLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
250 260
....*....|....*....|....*...
gi 1403710885 238 TESAPTEILIESPHHPYTQALINAVPDF 265
Cdd:COG1124 218 VEELTVADLLAGPKHPYTRELLAASLAF 245
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-264 |
1.02e-49 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 174.12 E-value: 1.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 1 MALLDICNLNIEIQTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKENWII-TADRFRFHDVELLKLS 79
Cdd:PRK15134 3 QPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVyPSGDIRFHGESLLHAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 80 PHKRRKIVGKEISMIFQNPLSCLDPSRKIGKQLIQNIpnwtfknkwwkWFGWKKRR------AIELLHRVGIKDHRDIMA 153
Cdd:PRK15134 83 EQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVL-----------SLHRGMRReaargeILNCLDRVGIRQAAKRLT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 154 SYPNELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLY 233
Cdd:PRK15134 152 DYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQ 231
|
250 260 270
....*....|....*....|....*....|.
gi 1403710885 234 CGQNTESAPTEILIESPHHPYTQALINAVPD 264
Cdd:PRK15134 232 NGRCVEQNRAATLFSAPTHPYTQKLLNSEPS 262
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-321 |
8.95e-47 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 161.41 E-value: 8.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 3 LLDICNLNIEIQTSNGR---------IKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKenwiITADRFRFHDV 73
Cdd:PRK15079 8 LLEVADLKVHFDIKDGKqwfwqppktLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVK----ATDGEVAWLGK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 74 ELLKLSPHKRRKiVGKEISMIFQNPLSCLDPSRKIGkQLIQNiPNWTFKNKWWKWFGWKKRRAIELlhRVGIKDhrDIMA 153
Cdd:PRK15079 84 DLLGMKDDEWRA-VRSDIQMIFQDPLASLNPRMTIG-EIIAE-PLRTYHPKLSRQEVKDRVKAMML--KVGLLP--NLIN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 154 SYPNELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSND---IKSISewcDQIS 230
Cdd:PRK15079 157 RYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDlavVKHIS---DRVL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 231 VLYCGQNTESAPTEILIESPHHPYTQALINAVPDFTQPLGFKTKLGTLEGTVPILEQMPIGCRLGPRCPFAQKKCME-KP 309
Cdd:PRK15079 234 VMYLGHAVELGTYDEVYHNPLHPYTKALMSAVPIPDPDLERNKTIQLLEGELPSPINPPSGCVFRTRCPIAGPECAKtRP 313
|
330
....*....|..
gi 1403710885 310 RRLKIKQHEFSC 321
Cdd:PRK15079 314 VLEGSFRHAVSC 325
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-264 |
3.31e-46 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 164.47 E-value: 3.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 18 GRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKenwiiTADRFRFHDVELLKLSPHKRRKiVGKEISMIFQN 97
Cdd:COG4172 297 GHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-----SEGEIRFDGQDLDGLSRRALRP-LRRRMQVVFQD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 98 PLSCLDPSRKIGkQLI------QNIPnwtfknkwwKWFGWKKRRAIELLHRVGIKdhRDIMASYPNELTEGEGQKVMIAM 171
Cdd:COG4172 371 PFGSLSPRMTVG-QIIaeglrvHGPG---------LSAAERRARVAEALEEVGLD--PAARHRYPHEFSGGQRQRIAIAR 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 172 AVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCGQNTESAPTEILIESPH 251
Cdd:COG4172 439 ALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQ 518
|
250
....*....|...
gi 1403710885 252 HPYTQALINAVPD 264
Cdd:COG4172 519 HPYTRALLAAAPL 531
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-229 |
9.50e-44 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 150.58 E-value: 9.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 2 ALLDICNLNIEIQTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKS----LIAkviCnaikenwIITAD--RFRFHDVEL 75
Cdd:COG1136 3 PLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKStllnILG---G-------LDRPTsgEVLIDGQDI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 76 LKLSPHKRRKIVGKEISMIFQNP-----LSCLD----PsrkigkQLIQNIPnwtfknkwwkwFGWKKRRAIELLHRVGIK 146
Cdd:COG1136 73 SSLSERELARLRRRHIGFVFQFFnllpeLTALEnvalP------LLLAGVS-----------RKERRERARELLERVGLG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 147 DHRDimaSYPNELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDiKSISEWC 226
Cdd:COG1136 136 DRLD---HRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARA 211
|
...
gi 1403710885 227 DQI 229
Cdd:COG1136 212 DRV 214
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-281 |
1.07e-43 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 159.25 E-value: 1.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 3 LLDICNLNIEIQTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKENW-IITAD----RFRFHDV-ELL 76
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGgLVQCDkmllRRRSRQViELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 77 KLSPHKRRKIVGKEISMIFQNPLSCLDPSRKIGKQLIQNIpnwtfKNKWWKWFGWKKRRAIELLHRVGIKDHRDIMASYP 156
Cdd:PRK10261 92 EQSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESI-----RLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 157 NELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCGQ 236
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1403710885 237 NTESAPTEILIESPHHPYTQALINAVPdftqplgfktKLGTLEGT 281
Cdd:PRK10261 247 AVETGSVEQIFHAPQHPYTRALLAAVP----------QLGAMKGL 281
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
8-229 |
1.26e-42 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 147.25 E-value: 1.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 8 NLNIEIQTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKenwiITADRFRFHDVELLKLSPHKRRKIV 87
Cdd:cd03255 5 NLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDR----PTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 88 GKEISMIFQNP-----LSCLD----PsrkigkQLIQNIPNWTfknkwwkwfgwKKRRAIELLHRVGIKDHrdiMASYPNE 158
Cdd:cd03255 81 RRHIGFVFQSFnllpdLTALEnvelP------LLLAGVPKKE-----------RRERAEELLERVGLGDR---LNHYPSE 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1403710885 159 LTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIkSISEWCDQI 229
Cdd:cd03255 141 LSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRI 210
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
18-323 |
7.25e-42 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 148.57 E-value: 7.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 18 GRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVIcNAIKENwiiTADRFRFHDVELLKLSPHKRrKIVGKEISMIFQN 97
Cdd:PRK11308 26 RLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLL-TMIETP---TGGELYYQGQDLLKADPEAQ-KLLRQKIQIVFQN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 98 PLSCLDPSRKIGKQLIQniPnwtFKNKWWKWFGWKKRRAIELLHRVGIK-DHRDimaSYPNELTEGEGQKVMIAMAVANQ 176
Cdd:PRK11308 101 PYGSLNPRKKVGQILEE--P---LLINTSLSAAERREKALAMMAKVGLRpEHYD---RYPHMFSGGQRQRIAIARALMLD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 177 PRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCGQNTESAPTEILIESPHHPYTQ 256
Cdd:PRK11308 173 PDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQ 252
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1403710885 257 ALINAVPDFTqPLGFKTKLgTLEGTVPILEQMPIGCRLGPRCPFAQKKC-MEKPRRLKIKQHEFSCHY 323
Cdd:PRK11308 253 ALLSATPRLN-PDDRRERI-KLTGELPSPLNPPPGCAFNARCPRAFGRCrQEQPQLRDYDGRLVACFA 318
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
8-286 |
1.70e-41 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 147.92 E-value: 1.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 8 NLNIEIQTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVIcNAIKEnwiITADRFRFHDVELLKLSPHKRRKiV 87
Cdd:COG1135 6 NLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCI-NLLER---PTSGSVLVDGVDLTALSERELRA-A 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 88 GKEISMIFQ--NPLScldpSR-------------KIGKQLIQnipnwtfknkwwkwfgwkkRRAIELLHRVGIKDHRDim 152
Cdd:COG1135 81 RRKIGMIFQhfNLLS----SRtvaenvalpleiaGVPKAEIR-------------------KRVAELLELVGLSDKAD-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 153 aSYPNELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSND---IKSIsewCDQI 229
Cdd:COG1135 136 -AYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEmdvVRRI---CDRV 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1403710885 230 SVLYCGQNTESAPTEILIESPHHPYTQALINAVPDFTQPLGFKTKLGTLEGTVPILE 286
Cdd:COG1135 212 AVLENGRIVEQGPVLDVFANPQSELTRRFLPTVLNDELPEELLARLREAAGGGRLVR 268
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
8-250 |
1.13e-36 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 132.32 E-value: 1.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 8 NLNIEIQTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVIcNAIKENwiiTADRFRFHDVELLKLSPHKRRKIv 87
Cdd:cd03258 6 NVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCI-NGLERP---TSGSVLVDGTDLTLLSGKELRKA- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 88 GKEISMIFQ--NPLScldpSRKIgkqlIQNI--PnwtfKNKWWKWFGWKKRRAIELLHRVGIKDHRDimaSYPNELTEGE 163
Cdd:cd03258 81 RRRIGMIFQhfNLLS----SRTV----FENValP----LEIAGVPKAEIEERVLELLELVGLEDKAD---AYPAQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 164 GQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCGQNTESAPT 243
Cdd:cd03258 146 KQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTV 225
|
....*..
gi 1403710885 244 EILIESP 250
Cdd:cd03258 226 EEVFANP 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
18-246 |
1.92e-32 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 121.00 E-value: 1.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 18 GRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKenwiITADRFRFHDVELLKLSPHkrrKIVGKEISMIFQN 97
Cdd:cd03219 11 GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLR----PTSGSVLFDGEDITGLPPH---EIARLGIGRTFQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 98 P-----LSCLDPSRkIGKQLIQniPNWTFKNKWWKWFGWKKRRAIELLHRVGIKDHRDIMASypnELTEGEGQKVMIAMA 172
Cdd:cd03219 84 PrlfpeLTVLENVM-VAAQART--GSGLLLARARREEREARERAEELLERVGLADLADRPAG---ELSYGQQRRLEIARA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1403710885 173 VANQPRLLIADEPTNALESTTALQVFRLLSSMNQnQGTTILLTSNDIKSISEWCDQISVLYCGQN-TESAPTEIL 246
Cdd:cd03219 158 LATDPKLLLLDEPAAGLNPEETEELAELIRELRE-RGITVLLVEHDMDVVMSLADRVTVLDQGRViAEGTPDEVR 231
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-285 |
2.40e-32 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 123.37 E-value: 2.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 5 DICNLNIEIQTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVIcNAIKENwiiTADRFRFHDVELLKLSP---- 80
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCI-NLLERP---TSGRVLVDGQDLTALSEkelr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 81 HKRRKIvgkeiSMIFQ--NPLScldpSR-------------KIGKQLIQnipnwtfknkwwkwfgwkkRRAIELLHRVGI 145
Cdd:PRK11153 79 KARRQI-----GMIFQhfNLLS----SRtvfdnvalplelaGTPKAEIK-------------------ARVTELLELVGL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 146 KDHRDimaSYPNELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEW 225
Cdd:PRK11153 131 SDKAD---RYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRI 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1403710885 226 CDQISVLYCGQNTESAPTEILIESPHHPYTQALINAVPDFTQPLGFKTKLGTL--EGTVPIL 285
Cdd:PRK11153 208 CDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFIQSTLHLDLPEDYLARLQAEptTGSGPLL 269
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
4-261 |
8.03e-32 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 119.80 E-value: 8.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 4 LDICNLNIEIQtsngrIKIVDGVNLSLNEGEITGLVGESGSGKSLiakvICNAIKEnwIITADRFRFHDVELLKLSPHKR 83
Cdd:PRK10418 5 IELRNIALQAA-----QPLVHGVSLTLQRGRVLALVGGSGSGKSL----TCAAALG--ILPAGVRQTAGRVLLDGKPVAP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 84 RKIVGKEISMIFQNPLSCLDPSRKIGKQLIQNIpnwtfknkWWKWFGWKKRRAIELLHRVGIKDHRDIMASYPNELTEGE 163
Cdd:PRK10418 74 CALRGRKIATIMQNPRSAFNPLHTMHTHARETC--------LALGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 164 GQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCGQNTESAPT 243
Cdd:PRK10418 146 LQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDV 225
|
250
....*....|....*...
gi 1403710885 244 EILIESPHHPYTQALINA 261
Cdd:PRK10418 226 ETLFNAPKHAVTRSLVSA 243
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-246 |
1.06e-31 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 119.76 E-value: 1.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 1 MALLDICNLNIEIqtsnGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKenwiITADRFRFHDVELLKLSP 80
Cdd:COG0411 2 DPLLEVRGLTKRF----GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYR----PTSGRILFDGRDITGLPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 81 HkrrKIVGKEISMIFQNP-----LSCLD-----PSRKIGKQLIQNIPNWtfkNKWWKWFGWKKRRAIELLHRVGIKDHRD 150
Cdd:COG0411 74 H---RIARLGIARTFQNPrlfpeLTVLEnvlvaAHARLGRGLLAALLRL---PRARREEREARERAEELLERVGLADRAD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 151 IMASypnELTEGEGQKVMIAMAVANQPRLLIADEPT---NALESTtalQVFRLLSSMNQNQGTTILLTSNDIKSISEWCD 227
Cdd:COG0411 148 EPAG---NLSYGQQRRLEIARALATEPKLLLLDEPAaglNPEETE---ELAELIRRLRDERGITILLIEHDMDLVMGLAD 221
|
250 260
....*....|....*....|
gi 1403710885 228 QISVLYCGQN-TESAPTEIL 246
Cdd:COG0411 222 RIVVLDFGRViAEGTPAEVR 241
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
10-232 |
2.22e-31 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 117.57 E-value: 2.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 10 NIEIQTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKEnwiiTADRFRFHDVELLKLSPHKRRKIVGk 89
Cdd:cd03225 4 NLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGP----TSGEVLVDGKDLTKLSLKELRRKVG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 90 eisMIFQNP---LSCLDpsrkIGKQLIQNIPNWtfknkwWKWFGWKKRRAIELLHRVGIKDHRDimaSYPNELTEGEGQK 166
Cdd:cd03225 79 ---LVFQNPddqFFGPT----VEEEVAFGLENL------GLPEEEIEERVEEALELVGLEGLRD---RSPFTLSGGQKQR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1403710885 167 VMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQnQGTTILLTSNDIKSISEWCDQISVL 232
Cdd:cd03225 143 VAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKA-EGKTIIIVTHDLDLLLELADRVIVL 207
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-187 |
2.37e-31 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 115.44 E-value: 2.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 23 VDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKEnwiiTADRFRFHDVELlklsPHKRRKIVGKEISMIFQNPlsCL 102
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSP----TEGTILLDGQDL----TDDERKSLRKEIGYVFQDP--QL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 103 DPSRKIGKQLIQNIPNWTFknkwwkWFGWKKRRAIELLHRVGIKDHRD-IMASYPNELTEGEGQKVMIAMAVANQPRLLI 181
Cdd:pfam00005 71 FPRLTVRENLRLGLLLKGL------SKREKDARAEEALEKLGLGDLADrPVGERPGTLSGGQRQRVAIARALLTKPKLLL 144
|
....*.
gi 1403710885 182 ADEPTN 187
Cdd:pfam00005 145 LDEPTA 150
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
10-229 |
1.68e-30 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 116.13 E-value: 1.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 10 NIEIQTSNGRiKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIkenwIITADRFRFHDVELLKLSPHKRRKiVGK 89
Cdd:cd03256 5 NLSKTYPNGK-KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLV----EPTSGSVLIDGTDINKLKGKALRQ-LRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 90 EISMIFQNPlscldpsRKIGKQ-LIQNI-----PNW-TFKNKWWKWFGWKKRRAIELLHRVGIKDHRDIMASypnELTEG 162
Cdd:cd03256 79 QIGMIFQQF-------NLIERLsVLENVlsgrlGRRsTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRAD---QLSGG 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1403710885 163 EGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQI 229
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRI 215
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-263 |
1.69e-29 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 119.19 E-value: 1.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 23 VDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIK-ENWIITADRFRFHDVELLKLSPHKRrkivgkEISMIFQNPLSC 101
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVEsQGGEIIFNGQRIDTLSPGKLQALRR------DIQFIFQDPYAS 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 102 LDPSRKIGKQLIQNIpnwtfKNKWWKWFGWKKRRAIELLHRVGIK-DHrdiMASYPNELTEGEGQKVMIAMAVANQPRLL 180
Cdd:PRK10261 414 LDPRQTVGDSIMEPL-----RVHGLLPGKAAAARVAWLLERVGLLpEH---AWRYPHEFSGGQRQRICIARALALNPKVI 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 181 IADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCGQNTESAPTEILIESPHHPYTQALIN 260
Cdd:PRK10261 486 IADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMA 565
|
...
gi 1403710885 261 AVP 263
Cdd:PRK10261 566 AVP 568
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
18-236 |
1.94e-29 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 112.85 E-value: 1.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 18 GRIKIVDGVNLSLNEGEITGLVGESGSGKS-LIaKVICNAIKenwiITADRfrfhdVELLKLSPHKRRKIVGKEISMIFQ 96
Cdd:COG1131 11 GDKTALDGVSLTVEPGEIFGLLGPNGAGKTtTI-RMLLGLLR----PTSGE-----VRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 97 NPlsCLDPSRKIGKQL-----IQNIPnwtfknkwwkwFGWKKRRAIELLHRVGIKDHRDIMASypnELTEGEGQKVMIAM 171
Cdd:COG1131 81 EP--ALYPDLTVRENLrffarLYGLP-----------RKEARERIDELLELFGLTDAADRKVG---TLSGGMKQRLGLAL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1403710885 172 AVANQPRLLIADEPTNALESTTALQVFRLLSSMNQnQGTTILLTSNDIKSISEWCDQISVLYCGQ 236
Cdd:COG1131 145 ALLHDPELLILDEPTSGLDPEARRELWELLRELAA-EGKTVLLSTHYLEEAERLCDRVAIIDKGR 208
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-262 |
2.41e-29 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 113.63 E-value: 2.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 1 MALLDICNLNIEIQTSN-----GRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKEnwiiTADRFRFHDVEL 75
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGGlsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESP----SQGNVSWRGEPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 76 LKLSpHKRRKIVGKEISMIFQNPLSCLDPSRKIGKQLIQNIPNWTfknkwWKWFGWKKRRAIELLHRVGIKDhrDIMASY 155
Cdd:PRK10419 77 AKLN-RAQRKAFRRDIQMVFQDSISAVNPRKTVREIIREPLRHLL-----SLDKAERLARASEMLRAVDLDD--SVLDKR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 156 PNELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCG 235
Cdd:PRK10419 149 PPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNG 228
|
250 260
....*....|....*....|....*..
gi 1403710885 236 QNTESAPTEILIeSPHHPYTQALINAV 262
Cdd:PRK10419 229 QIVETQPVGDKL-TFSSPAGRVLQNAV 254
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
18-218 |
2.96e-29 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 112.07 E-value: 2.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 18 GRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKenwiITADRFRFHDVELLKLSPHK----RRKIvGkeisM 93
Cdd:COG2884 13 GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEER----PTSGQVLVNGQDLSRLKRREipylRRRI-G----V 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 94 IFQN---------------PLSCLDPSRKIgkqlIQnipnwtfknkwwkwfgwkkRRAIELLHRVGIKDHRDimaSYPNE 158
Cdd:COG2884 84 VFQDfrllpdrtvyenvalPLRVTGKSRKE----IR-------------------RRVREVLDLVGLSDKAK---ALPHE 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 159 LTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNqGTTILLTSND 218
Cdd:COG2884 138 LSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHD 196
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
11-259 |
1.80e-27 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 107.76 E-value: 1.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 11 IEIQ---TSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKenwiITADRFRFHDVELLKLSPHKRRKIV 87
Cdd:COG1127 6 IEVRnltKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLR----PDSGEILVDGQDITGLSEKELYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 88 gKEISMIFQNP-----LSCLD----PSR---KIGKQLIQnipnwtfknkwwkwfgwkkRRAIELLHRVGIKDHRDIMasy 155
Cdd:COG1127 82 -RRIGMLFQGGalfdsLTVFEnvafPLRehtDLSEAEIR-------------------ELVLEKLELVGLPGAADKM--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 156 PNELTEGEgQK-VMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYC 234
Cdd:COG1127 139 PSELSGGM-RKrVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLAD 217
|
250 260
....*....|....*....|....*
gi 1403710885 235 GQNTESAPTEILIESPhHPYTQALI 259
Cdd:COG1127 218 GKIIAEGTPEELLASD-DPWVRQFL 241
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-259 |
1.84e-27 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 112.49 E-value: 1.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 3 LLDICNLNIEIQTSNGRIK-------IVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKENWIITADRFRFHDVEL 75
Cdd:PRK15134 275 LLDVEQLQVAFPIRKGILKrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIWFDGQPLHNLNR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 76 LKLSPHKRRkivgkeISMIFQNPLSCLDPSRKIgkqlIQNIPNWTFKNKWWKWFGWKKRRAIELLHRVGI---KDHRdim 152
Cdd:PRK15134 355 RQLLPVRHR------IQVVFQDPNSSLNPRLNV----LQIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLdpeTRHR--- 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 153 asYPNELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVL 232
Cdd:PRK15134 422 --YPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVL 499
|
250 260
....*....|....*....|....*..
gi 1403710885 233 YCGQNTESAPTEILIESPHHPYTQALI 259
Cdd:PRK15134 500 RQGEVVEQGDCERVFAAPQQEYTRQLL 526
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
16-236 |
3.45e-27 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 105.21 E-value: 3.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 16 SNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKenwiITADRFRFHDVELLKLSPHKRRKIvgkeISMIF 95
Cdd:cd03214 8 GYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLK----PSSGEILLDGKDLASLSPKELARK----IAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 96 QnplscldpsrkigkqliqnipnwtfknkwwkwfgwkkrraieLLHRVGIKD--HRDImasypNELTEGEGQKVMIAMAV 173
Cdd:cd03214 80 Q------------------------------------------ALELLGLAHlaDRPF-----NELSGGERQRVLLARAL 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1403710885 174 ANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCGQ 236
Cdd:cd03214 113 AQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGR 175
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
11-251 |
1.28e-26 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 105.28 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 11 IEIQ---TSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKEnwiiTADRFRFHDVELLKLSPHKRRKIv 87
Cdd:cd03261 1 IELRgltKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRP----DSGEVLIDGEDISGLSEAELYRL- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 88 GKEISMIFQNP-----LSCLD----PSR---KIGKQLIQnipnwtfknkwwkwfgwkkRRAIELLHRVGIKDHRDimaSY 155
Cdd:cd03261 76 RRRMGMLFQSGalfdsLTVFEnvafPLRehtRLSEEEIR-------------------EIVLEKLEAVGLRGAED---LY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 156 PNELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCG 235
Cdd:cd03261 134 PAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDG 213
|
250
....*....|....*.
gi 1403710885 236 QNTESAPTEILIESPH 251
Cdd:cd03261 214 KIVAEGTPEELRASDD 229
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-262 |
1.37e-26 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 105.90 E-value: 1.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 3 LLDICNLNIEIqtsnGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKenwiITADRFRFHDVELLKLSPHK 82
Cdd:COG1120 1 MLEAENLSVGY----GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLK----PSSGEVLLDGRDLASLSRRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 83 RRKIVGkeisMIFQN-----PLSCLD-------PSRKIGKQLiqnipnwtfknkwwkwfGWKKRRAI-ELLHRVGIKD-- 147
Cdd:COG1120 73 LARRIA----YVPQEppapfGLTVRElvalgryPHLGLFGRP-----------------SAEDREAVeEALERTGLEHla 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 148 HRDImasypNELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCD 227
Cdd:COG1120 132 DRPV-----DELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYAD 206
|
250 260 270
....*....|....*....|....*....|....*.
gi 1403710885 228 QISVLYCGQNTES-APTEILiesphhpyTQALINAV 262
Cdd:COG1120 207 RLVLLKDGRIVAQgPPEEVL--------TPELLEEV 234
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
18-236 |
1.69e-26 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 102.71 E-value: 1.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 18 GRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKenwiITADRFRFHDVELLKLSPHKRRKivgkEISMIFQn 97
Cdd:cd00267 10 GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK----PTSGEILIDGKDIAKLPLEELRR----RIGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 98 plscldpsrkigkqliqnipnwtfknkwwkwfgwkkrraiellhrvgikdhrdimasypneLTEGEGQKVMIAMAVANQP 177
Cdd:cd00267 81 -------------------------------------------------------------LSGGQRQRVALARALLLNP 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1403710885 178 RLLIADEPTNALESTTALQVFRLLSSMNQnQGTTILLTSNDIKSISEWCDQISVLYCGQ 236
Cdd:cd00267 100 DLLLLDEPTSGLDPASRERLLELLRELAE-EGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
18-236 |
5.27e-26 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 102.09 E-value: 5.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 18 GRIKIVDGVNLSLNEGEITGLVGESGSGKS-LIaKVICNaikenwIITADRfrfHDVELLKLSPHKRRKIVGKEISMIFQ 96
Cdd:cd03230 11 GKKTALDDISLTVEKGEIYGLLGPNGAGKTtLI-KIILG------LLKPDS---GEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 97 NPlscldpsrkigkqliQNIPNWTfknkwwkwfgwkkrrAIELLhrvgikdhrdimasypnELTEGEGQKVMIAMAVANQ 176
Cdd:cd03230 81 EP---------------SLYENLT---------------VRENL-----------------KLSGGMKQRLALAQALLHD 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 177 PRLLIADEPTNALESTTALQVFRLLSSMNQnQGTTILLTSNDIKSISEWCDQISVLYCGQ 236
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRELKK-EGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
20-218 |
1.80e-25 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 101.72 E-value: 1.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 20 IKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKEnwiiTADRFRFHDVELLKLsphKRRKI--VGKEISMIFQN 97
Cdd:cd03292 14 TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELP----TSGTIRVNGQDVSDL---RGRAIpyLRRKIGVVFQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 98 plSCLDPSRKIGKqliqnipNWTFKNKWWKWFGWKKR-RAIELLHRVGIKDHRDimaSYPNELTEGEGQKVMIAMAVANQ 176
Cdd:cd03292 87 --FRLLPDRNVYE-------NVAFALEVTGVPPREIRkRVPAALELVGLSHKHR---ALPAELSGGEQQRVAIARAIVNS 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1403710885 177 PRLLIADEPTNALESTTALQVFRLLSSMNQnQGTTILLTSND 218
Cdd:cd03292 155 PTILIADEPTGNLDPDTTWEIMNLLKKINK-AGTTVVVATHA 195
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-218 |
2.57e-25 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 101.74 E-value: 2.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 2 ALLDICNLNIEIQTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKS----LIAKVicnaikEnwIITADRFRFHDVELLK 77
Cdd:COG4181 7 PIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKStllgLLAGL------D--RPTSGTVRLAGQDLFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 78 LSPHKRRKIVGKEISMIFQNplscldpsrkigKQLIqniPNWT-----------------FknkwwkwfgwkkRRAIELL 140
Cdd:COG4181 79 LDEDARARLRARHVGFVFQS------------FQLL---PTLTalenvmlplelagrrdaR------------ARARALL 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1403710885 141 HRVGIKdHRdiMASYPNELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSND 218
Cdd:COG4181 132 ERVGLG-HR--LDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHD 206
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
14-219 |
1.54e-24 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 99.47 E-value: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 14 QTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKenwiITADRFRFHDVELLKLSPHkrrkivgkeISM 93
Cdd:cd03293 11 GGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLER----PTSGEVLVDGEPVTGPGPD---------RGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 94 IFQNPLscLDPSRKIgkqlIQNIpnwTFKNKWWKWFGWKKR-RAIELLHRVGIKDHRDimaSYPNELTEGEGQKVMIAMA 172
Cdd:cd03293 78 VFQQDA--LLPWLTV----LDNV---ALGLELQGVPKAEAReRAEELLELVGLSGFEN---AYPHQLSGGMRQRVALARA 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1403710885 173 VANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDI 219
Cdd:cd03293 146 LAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDI 192
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
239-305 |
1.08e-23 |
|
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found towards the C-terminus of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid.
Pssm-ID: 400588 [Multi-domain] Cd Length: 65 Bit Score: 92.46 E-value: 1.08e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1403710885 239 ESAPTEILIESPHHPYTQALINAVPDFTQPlgfKTKLGTLEGTVPILEQMPIGCRLGPRCPFAQKKC 305
Cdd:pfam08352 2 EEGPTDDILENPLHPYTRALLNSVPRLDPP---KRPLYTIPGNVPSLLELPEGCPFAPRCPFATEEC 65
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
22-232 |
4.20e-23 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 95.29 E-value: 4.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 22 IVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKenwiitADRFRfhdVELLKLSPHKRRKIVG-----KEISMIFq 96
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLK------PTSGS---IRVFGKPLEKERKRIGyvpqrRSIDRDF- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 97 nPLSCLDpsrkigkqlIQNIPNWTFKNKWWKWFGWKKRRAIELLHRVGIKDHRD--ImasypNELTEGEGQKVMIAMAVA 174
Cdd:cd03235 84 -PISVRD---------VVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADrqI-----GELSGGQQQRVLLARALV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1403710885 175 NQPRLLIADEPTNALESTTALQVFRLLSSMNQnQGTTILLTSNDIKSISEWCDQISVL 232
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDIYELLRELRR-EGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
18-248 |
4.74e-23 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 99.88 E-value: 4.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 18 GRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIK----ENWIITADRFrfhdVELLKLSPHKRRKiVGKEISM 93
Cdd:TIGR03269 295 GVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEptsgEVNVRVGDEW----VDMTKPGPDGRGR-AKRYIGI 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 94 IFQNplSCLDPSRKIgkqliqnIPNWTFKNKWWKWFGWKKRRAIELLHRVGIKDH--RDIMASYPNELTEGEGQKVMIAM 171
Cdd:TIGR03269 370 LHQE--YDLYPHRTV-------LDNLTEAIGLELPDELARMKAVITLKMVGFDEEkaEEILDKYPDELSEGERHRVALAQ 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1403710885 172 AVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCGQNTESAPTEILIE 248
Cdd:TIGR03269 441 VLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
2-262 |
1.75e-22 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 94.90 E-value: 1.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 2 ALLDICNLNieiqTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICN--AIKENWIITADRFRfHDVELLKLS 79
Cdd:TIGR02323 2 PLLQVSGLS----KSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGrlAPDHGTATYIMRSG-AELELYQLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 80 PHKRRKIVGKEISMIFQNPLSCL----DPSRKIGKQLIqnipnwtfkNKWWKWFGWKKRRAIELLHRVGIKDHRdiMASY 155
Cdd:TIGR02323 77 EAERRRLMRTEWGFVHQNPRDGLrmrvSAGANIGERLM---------AIGARHYGNIRATAQDWLEEVEIDPTR--IDDL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 156 PNELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCG 235
Cdd:TIGR02323 146 PRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQG 225
|
250 260
....*....|....*....|....*..
gi 1403710885 236 QNTESAPTEILIESPHHPYTQALINAV 262
Cdd:TIGR02323 226 RVVESGLTDQVLDDPQHPYTQLLVSSI 252
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-246 |
1.97e-22 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 93.78 E-value: 1.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 4 LDICNLNIEIqtsnGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKENWIITAD---RFRFHDVELLKLSP 80
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEgevLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 81 HKRRKIVGkeisMIFQNPlsclDPSRK-------IGKQLIQNIPNwtfknkwwkwfGWKKRRAIELLHRVGIKD--HRDI 151
Cdd:cd03260 77 LELRRRVG----MVFQKP----NPFPGsiydnvaYGLRLHGIKLK-----------EELDERVEEALRKAALWDevKDRL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 152 MASypnELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNqgTTILLTSNDIKSISEWCDQISV 231
Cdd:cd03260 138 HAL---GLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAF 212
|
250
....*....|....*
gi 1403710885 232 LYCGQNTESAPTEIL 246
Cdd:cd03260 213 LLNGRLVEFGPTEQI 227
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
18-232 |
4.27e-22 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 92.58 E-value: 4.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 18 GRIKIVDGVNLSLNEGEITGLVGESGSGKS----LIAKVIcnaikenwIITADRFRFHDVELLKLSPHKRRkivgkeISM 93
Cdd:cd03259 11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTtllrLIAGLE--------RPDSGEILIDGRDVTGVPPERRN------IGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 94 IFQNPlsCLDPS-------------RKIGKQLIQnipnwtfknkwwkwfgwkkRRAIELLHRVGIKDHRDimaSYPNELT 160
Cdd:cd03259 77 VFQDY--ALFPHltvaeniafglklRGVPKAEIR-------------------ARVRELLELVGLEGLLN---RYPHELS 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1403710885 161 EGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVL 232
Cdd:cd03259 133 GGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVM 204
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
17-261 |
8.28e-22 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 92.75 E-value: 8.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 17 NGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVIcnaikeNWIITAD--RFRFHDVELLKLSPHK-RRKIvGKEISM 93
Cdd:cd03295 11 GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMI------NRLIEPTsgEIFIDGEDIREQDPVElRRKI-GYVIQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 94 IfqnplsCLDPSRKIgkqlIQNIPnwTFKNKWWKWFGWKKRRAIELLHRVGIkDHRDIMASYPNELTEGEGQKVMIAMAV 173
Cdd:cd03295 84 I------GLFPHMTV----EENIA--LVPKLLKWPKEKIRERADELLALVGL-DPAEFADRYPHELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 174 ANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCGQNTESAPTEILIESPHHP 253
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPAND 230
|
....*...
gi 1403710885 254 YTQALINA 261
Cdd:cd03295 231 FVAEFVGA 238
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
18-236 |
9.35e-22 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 90.71 E-value: 9.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 18 GRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKenwiITADRFRFHDVELLKLS----PHKRRkivgkeISM 93
Cdd:cd03229 11 GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEE----PDSGSILIDGEDLTDLEdelpPLRRR------IGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 94 IFQNPlsCLDPSRKIgkqlIQNIpnwtfknkwwkwfgwkkrraiellhrvgikdhrdimaSYPneLTEGEGQKVMIAMAV 173
Cdd:cd03229 81 VFQDF--ALFPHLTV----LENI-------------------------------------ALG--LSGGQQQRVALARAL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1403710885 174 ANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCGQ 236
Cdd:cd03229 116 AMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
3-220 |
1.95e-21 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 91.42 E-value: 1.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 3 LLDICNLNIEIQTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKEnwiiTADRFRFHDVELLKLSPHK 82
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTP----TSGDVIFNGQPMSKLSSAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 83 RRKIVGKEISMIFQ--------NPLSCLDPSRKIGKQLIQNIpnwtfknkwwkwfgwkKRRAIELLHRVGIK---DHRdi 151
Cdd:PRK11629 81 KAELRNQKLGFIYQfhhllpdfTALENVAMPLLIGKKKPAEI----------------NSRALEMLAAVGLEhraNHR-- 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1403710885 152 masyPNELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIK 220
Cdd:PRK11629 143 ----PSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQ 207
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
239-323 |
3.17e-21 |
|
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model represents a domain found in the C-terminal regions of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 213647 [Multi-domain] Cd Length: 87 Bit Score: 86.65 E-value: 3.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 239 ESAPTEILIESPHHPYTQALINAVPDFTQPlgfKTKLGTLEGTVPILEQMPIGCRLGPRCPFAQKKCMEKPRRLK--IKQ 316
Cdd:TIGR01727 4 ETGPAEEIFKNPLHPYTKALLSAIPTIKKR---DRKLISIPGEVPSLINLPSGCRFYPRCPYAQDECRKEPPALVeiAEG 80
|
....*..
gi 1403710885 317 HEFSCHY 323
Cdd:TIGR01727 81 HRVACHL 87
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-236 |
3.20e-21 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 88.64 E-value: 3.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 18 GRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKenwiITADRFRFHDVELLKLSPHKRRKIvGkeISMIFQn 97
Cdd:cd03216 11 GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYK----PDSGEILVDGKEVSFASPRDARRA-G--IAMVYQ- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 98 plscldpsrkigkqliqnipnwtfknkwwkwfgwkkrraiellhrvgikdhrdimasypneLTEGEGQKVMIAMAVANQP 177
Cdd:cd03216 83 -------------------------------------------------------------LSVGERQMVEIARALARNA 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1403710885 178 RLLIADEPTNALESTTALQVFRLLSSMnQNQGTTILLTSNDIKSISEWCDQISVLYCGQ 236
Cdd:cd03216 102 RLLILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGR 159
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
13-219 |
8.59e-21 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 89.13 E-value: 8.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 13 IQTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVIcNAIKEnwiITADRFRFHDVELLKlsPHKRRKIVGKEIS 92
Cdd:cd03262 6 LHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCI-NLLEE---PDSGTIIIDGLKLTD--DKKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 93 MIFQNplSCLDPSRKIgkqlIQNI---PNWTFKNKWWKWFgwkkRRAIELLHRVGIKDHRDimaSYPNELTEGEGQKVMI 169
Cdd:cd03262 80 MVFQQ--FNLFPHLTV----LENItlaPIKVKGMSKAEAE----ERALELLEKVGLADKAD---AYPAQLSGGQQQRVAI 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1403710885 170 AMAVANQPRLLIADEPTNALESTTALQVfrlLSSMNQ--NQGTTILLTSNDI 219
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDPELVGEV---LDVMKDlaEEGMTMVVVTHEM 195
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-261 |
1.00e-20 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 90.23 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 3 LLDICNLNIEIQTSNG-----RIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKE---NWIITADRFRFHDVe 74
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPtsgELLIDDHPLHFGDY- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 75 llklspHKRrkivGKEISMIFQNPLSCLDPSRKIGKQLiqNIPnwtFKNKWWKWFGWKKRRAIELLHRVGIKdhRDIMAS 154
Cdd:PRK15112 83 ------SYR----SQRIRMIFQDPSTSLNPRQRISQIL--DFP---LRLNTDLEPEQREKQIIETLRQVGLL--PDHASY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 155 YPNELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYC 234
Cdd:PRK15112 146 YPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQ 225
|
250 260
....*....|....*....|....*..
gi 1403710885 235 GQNTESAPTEILIESPHHPYTQALINA 261
Cdd:PRK15112 226 GEVVERGSTADVLASPLHELTKRLIAG 252
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
17-229 |
2.20e-20 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 87.70 E-value: 2.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 17 NGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKEnwiiTADRFRFHDVellKLSPHKRRKIVGkeisMIFQ 96
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKE----SSGSILLNGK---PIKAKERRKSIG----YVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 97 NPLSCLDpSRKIGKQLIQNIPNwtfknkwwkwFGWKKRRAIELLHRVGIKDHRDimaSYPNELTEGEGQKVMIAMAVANQ 176
Cdd:cd03226 79 DVDYQLF-TDSVREELLLGLKE----------LDAGNEQAETVLKDLDLYALKE---RHPLSLSGGQKQRLAIAAALLSG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1403710885 177 PRLLIADEPTNALESTTALQVFRLLSSMnQNQGTTILLTSNDIKSISEWCDQI 229
Cdd:cd03226 145 KDLLIFDEPTSGLDYKNMERVGELIREL-AAQGKAVIVITHDYEFLAKVCDRV 196
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
13-245 |
5.10e-20 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 87.04 E-value: 5.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 13 IQTSN-----GRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIK----ENWIITadrfrfHDVEllklsphKR 83
Cdd:cd03265 1 IEVENlvkkyGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKptsgRATVAG------HDVV-------RE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 84 RKIVGKEISMIFQNPlsCLDPSRKIGKQL-----IQNIPNwtfknkwwkwfGWKKRRAIELLHRVGIKDHRDIMASYpne 158
Cdd:cd03265 68 PREVRRRIGIVFQDL--SVDDELTGWENLyiharLYGVPG-----------AERRERIDELLDFVGLLEAADRLVKT--- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 159 LTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCGQ-N 237
Cdd:cd03265 132 YSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRiI 211
|
....*...
gi 1403710885 238 TESAPTEI 245
Cdd:cd03265 212 AEGTPEEL 219
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
18-223 |
6.65e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 86.85 E-value: 6.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 18 GRiKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKEnwiiTADRFRF--HDVELLKLS--PHKRRkivgkEISM 93
Cdd:PRK10908 14 GR-QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERP----SAGKIWFsgHDITRLKNRevPFLRR-----QIGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 94 IFQNPLSCLDPS--RKIGKQLIqnipnwtfknKWWKWFGWKKRRAIELLHRVGIKDHrdiMASYPNELTEGEGQKVMIAM 171
Cdd:PRK10908 84 IFQDHHLLMDRTvyDNVAIPLI----------IAGASGDDIRRRVSAALDKVGLLDK---AKNFPIQLSGGEQQRVGIAR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1403710885 172 AVANQPRLLIADEPTNALESTTALQVFRLLSSMNQnQGTTILLTSNDIKSIS 223
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLIS 201
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
12-263 |
1.12e-19 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 87.31 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 12 EIQTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKenwiITADRFRFHDVELLKLSPHKRRKIVGKEI 91
Cdd:cd03294 29 EILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIE----PTSGKVLIDGQDIAAMSRKELRELRRKKI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 92 SMIFQNplSCLDPSRKIGKQL-----IQNIPnwtfknkwwkwFGWKKRRAIELLHRVGIKDHRDimaSYPNELTEGEGQK 166
Cdd:cd03294 105 SMVFQS--FALLPHRTVLENVafgleVQGVP-----------RAEREERAAEALELVGLEGWEH---KYPDELSGGMQQR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 167 VMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCGQNTESAPTEIL 246
Cdd:cd03294 169 VGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEI 248
|
250
....*....|....*..
gi 1403710885 247 IESPHHPYTQALINAVP 263
Cdd:cd03294 249 LTNPANDYVREFFRGVD 265
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
18-218 |
3.24e-19 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 84.98 E-value: 3.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 18 GRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKenwiITADRFRFHDVELLKLSPHKRRkivgkeISMIFQN 97
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFET----PTSGEILLDGKDITNLPPHKRP------VNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 98 ---------------PLSCldpsRKIGKQLIQnipnwtfknkwwkwfgwkkRRAIELLHRVGIKDHRDimaSYPNELTEG 162
Cdd:cd03300 81 yalfphltvfeniafGLRL----KKLPKAEIK-------------------ERVAEALDLVQLEGYAN---RKPSQLSGG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1403710885 163 EGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSND 218
Cdd:cd03300 135 QQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHD 190
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
22-248 |
3.68e-19 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 88.74 E-value: 3.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 22 IVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKenwiITADRFRFHDVELLKLSPHKRRKIVGkeisMIFQNPL-- 99
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYE----PTSGRILIDGIDLRQIDPASLRRQIG----VVLQDVFlf 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 100 --ScldpsrkigkqLIQNI----PNWTFKnkwwkwfgwkkrRAIELLHRVGIkdHRDIMAsYPN----ELTE-------G 162
Cdd:COG2274 562 sgT-----------IRENItlgdPDATDE------------EIIEAARLAGL--HDFIEA-LPMgydtVVGEggsnlsgG 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 163 EGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQgTTILLTSNDikSISEWCDQISVLYCGQNTESAP 242
Cdd:COG2274 616 QRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGR-TVIIIAHRL--STIRLADRIIVLDKGRIVEDGT 692
|
....*.
gi 1403710885 243 TEILIE 248
Cdd:COG2274 693 HEELLA 698
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
18-250 |
6.23e-19 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 84.76 E-value: 6.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 18 GRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVIcNAIKEnwiITADRFRfhdVELLK-LSPHKRRKIVGKEISMIFQ 96
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCI-NKLEE---ITSGDLI---VDGLKvNDPKVDERLIRQEAGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 97 N----P-LSCLD-----P--SRKIGKQliqnipnwtfknkwwkwfgWKKRRAIELLHRVGIKDHrdiMASYPNELTEGEG 164
Cdd:PRK09493 85 QfylfPhLTALEnvmfgPlrVRGASKE-------------------EAEKQARELLAKVGLAER---AHHYPSELSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 165 QKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMnQNQGTTILLTSNDIKSISEWCDQISVLYCGQNTESAPTE 244
Cdd:PRK09493 143 QRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQ 221
|
....*.
gi 1403710885 245 ILIESP 250
Cdd:PRK09493 222 VLIKNP 227
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
32-236 |
8.36e-19 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 83.50 E-value: 8.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 32 EGEITGLVGESGSGKSLIAKVICNAIKenwiITADRFRFHDVEL------LKLSPHKRRkivgkeISMIFQNplSCLDPS 105
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEK----PDGGTIVLNGTVLfdsrkkINLPPQQRK------IGLVFQQ--YALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 106 RKIgkqlIQNIpnwTFKNKWWKWFGWKKRRAiELLHRVGIkDHrdIMASYPNELTEGEGQKVMIAMAVANQPRLLIADEP 185
Cdd:cd03297 90 LNV----RENL---AFGLKRKRNREDRISVD-ELLDLLGL-DH--LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1403710885 186 TNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCGQ 236
Cdd:cd03297 159 FSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
24-244 |
8.86e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 87.00 E-value: 8.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 24 DGVNLSLNEGEITGLVGESGSGKS-LIaKVICNaikenwIITAD--RFRFHDVELLKLSPHKRRKIvGkeISMIFQNPLs 100
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKStLM-KILSG------VYQPDsgEILLDGEPVRFRSPRDAQAA-G--IAIIHQELN- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 101 cLDPSRKIGkqliQNI-----P------NWtfknkwwkwfGWKKRRAIELLHRVGIK-DHRDIMAsypnELTEGEGQKVM 168
Cdd:COG1129 90 -LVPNLSVA----ENIflgrePrrggliDW----------RAMRRRARELLARLGLDiDPDTPVG----DLSVAQQQLVE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1403710885 169 IAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMnQNQGTTILLTS---NDIKSIsewCDQISVLYCGQNTESAPTE 244
Cdd:COG1129 151 IARALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYIShrlDEVFEI---ADRVTVLRDGRLVGTGPVA 225
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
11-260 |
4.25e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 82.71 E-value: 4.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 11 IEIQTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIK--ENWIITADR----FRFHDVELlKLSPHKRR 84
Cdd:PRK10619 9 IDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKpsEGSIVVNGQtinlVRDKDGQL-KVADKNQL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 85 KIVGKEISMIFQ--NPLSCLDPSRKIGKQLIQNIpnwtfknkwWKWFGWKKRRAIELLHRVGIKDHRDimASYPNELTEG 162
Cdd:PRK10619 88 RLLRTRLTMVFQhfNLWSHMTVLENVMEAPIQVL---------GLSKQEARERAVKYLAKVGIDERAQ--GKYPVHLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 163 EGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQnQGTTILLTSNDIKSISEWCDQISVLYCGQNTESAP 242
Cdd:PRK10619 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAE-EGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGA 235
|
250
....*....|....*...
gi 1403710885 243 TEILIESPHHPYTQALIN 260
Cdd:PRK10619 236 PEQLFGNPQSPRLQQFLK 253
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
12-262 |
4.76e-18 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 82.15 E-value: 4.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 12 EIQTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKEnwiiTADRFRFHDVELLKLSPHKRrkivgkEI 91
Cdd:TIGR00968 5 NISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQP----DSGRIRLNGQDATRVHARDR------KI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 92 SMIFQN--PLSCLDPSRKIGKQL-IQNIPnwtfknkwwkwFGWKKRRAIELLHRVGIKDHRDimaSYPNELTEGEGQKVM 168
Cdd:TIGR00968 75 GFVFQHyaLFKHLTVRDNIAFGLeIRKHP-----------KAKIKARVEELLELVQLEGLGD---RYPNQLSGGQRQRVA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 169 IAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCGQNTE-SAPTEILi 247
Cdd:TIGR00968 141 LARALAVEPQVLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQiGSPDEVY- 219
|
250
....*....|....*
gi 1403710885 248 ESPHHPYTQALINAV 262
Cdd:TIGR00968 220 DHPANPFVMSFLGEV 234
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
21-232 |
9.11e-18 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 79.73 E-value: 9.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 21 KIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKenwiITADRFRFHDVELLKLSPHKRRKIvgkeISMIFQNPLs 100
Cdd:cd03228 16 PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYD----PTSGEILIDGVDLRDLDLESLRKN----IAYVPQDPF- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 101 cldpsrkigkqliqnipnwtfknkwwkwfgwkkrraieLLHRVgIKDhrdimasypNELTEGEGQKVMIAMAVANQPRLL 180
Cdd:cd03228 87 --------------------------------------LFSGT-IRE---------NILSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1403710885 181 IADEPTNALESTTALQVFRLLSSMnqNQGTTILLTSNDIKSISEwCDQISVL 232
Cdd:cd03228 119 ILDEATSALDPETEALILEALRAL--AKGKTVIVIAHRLSTIRD-ADRIIVL 167
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
23-236 |
1.29e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 81.75 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 23 VDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKEnwiiTADRFRFHDVELLKLSPHKRRKIVGKEISMIFQNPLSCL 102
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKP----TTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQFPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 103 ---DPSRKI---GKQLIQNIPNwtfknkwwkwfgwKKRRAIELLHRVGIKdhRDIMASYPNELTEGEGQKVMIAMAVANQ 176
Cdd:PRK13646 99 fedTVEREIifgPKNFKMNLDE-------------VKNYAHRLLMDLGFS--RDVMSQSPFQMSGGQMRKIAIVSILAMN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 177 PRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCGQ 236
Cdd:PRK13646 164 PDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGS 223
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
13-236 |
1.50e-17 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 79.95 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 13 IQTSN-----GRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKenwiITADRFRFHDVELLKLSPHKRRkiV 87
Cdd:cd03268 1 LKTNDltktyGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIK----PDSGEITFDGKSYQKNIEALRR--I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 88 GKEISM-IFQNPLSCLDPSRKIGKQLIqnIPNwtfknkwwkwfgwkkRRAIELLHRVGIKDHRDIMASypnELTEGEGQK 166
Cdd:cd03268 75 GALIEApGFYPNLTARENLRLLARLLG--IRK---------------KRIDEVLDVVGLKDSAKKKVK---GFSLGMKQR 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 167 VMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNqNQGTTILLTSNDIKSISEWCDQISVLYCGQ 236
Cdd:cd03268 135 LGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLR-DQGITVLISSHLLSEIQKVADRIGIINKGK 203
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-256 |
1.72e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 80.73 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 1 MALLDICNLNIeiqtSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIK---------ENWIITADRFRFH 71
Cdd:PRK14247 1 MNKIEIRDLKV----SFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypearvsgEVYLDGQDIFKMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 72 DVELlklsphKRRkivgkeISMIFQ--NPLSCLdpsrkigkQLIQNIPNWTFKNKWWKWFGWKKRRAIELLHRVGIKDH- 148
Cdd:PRK14247 77 VIEL------RRR------VQMVFQipNPIPNL--------SIFENVALGLKLNRLVKSKKELQERVRWALEKAQLWDEv 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 149 RDIMASYPNELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQgtTILLTSNDIKSISEWCDQ 228
Cdd:PRK14247 137 KDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDY 214
|
250 260
....*....|....*....|....*...
gi 1403710885 229 ISVLYCGQNTESAPTEILIESPHHPYTQ 256
Cdd:PRK14247 215 VAFLYKGQIVEWGPTREVFTNPRHELTE 242
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
16-236 |
2.02e-17 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 79.86 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 16 SNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKenwiITADrfrfhDVELLKLSPHKRRKIVGKEISMIF 95
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELR----PTSG-----TAYINGYSIRTDRKAARQSLGYCP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 96 QNP-----LSCLDPSRKIGkqLIQNIPNWTfknkwwkwfgwkKRRAIELLHR-VGIKDHRDIMASypnELTEGEGQKVMI 169
Cdd:cd03263 82 QFDalfdeLTVREHLRFYA--RLKGLPKSE------------IKEEVELLLRvLGLTDKANKRAR---TLSGGMKRKLSL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1403710885 170 AMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNqgTTILLTSNDIKSISEWCDQISVLYCGQ 236
Cdd:cd03263 145 AIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKG--RSIILTTHSMDEAEALCDRIAIMSDGK 209
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
20-232 |
2.37e-17 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 80.07 E-value: 2.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 20 IKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNaikenwIITADRFRfhdVELLKLSPHKRRKIVGKEISMIFqnpl 99
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSG------LLQPTSGE---VRVAGLVPWKRRKKFLRRIGVVF---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 100 scldpsrkiGK--QLIQNIPnwtfknkwwkwfgwkKRRAIELLHRV-GIKDHR---------------DIMASYPNELTE 161
Cdd:cd03267 101 ---------GQktQLWWDLP---------------VIDSFYLLAAIyDLPPARfkkrldelselldleELLDTPVRQLSL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1403710885 162 GEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVL 232
Cdd:cd03267 157 GQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVI 227
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
18-236 |
3.64e-17 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 78.86 E-value: 3.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 18 GRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVIcnaikeNWIITADRFRFHdVELLKLSPHKRRKI--VGKEismif 95
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMI------LGIILPDSGEVL-FDGKPLDIAARNRIgyLPEE----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 96 qnplSCLDPSRKIGKQLIQnipnwtFKNKWWKWFGWKKRRAIELLHRVGIKDHRDIMAsypNELTEGEGQKVMIAMAVAN 175
Cdd:cd03269 79 ----RGLYPKMKVIDQLVY------LAQLKGLKKEEARRRIDEWLERLELSEYANKRV---EELSKGNQQKVQFIAAVIH 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1403710885 176 QPRLLIADEPTNALESTTALQVFRLLSSMnQNQGTTILLTSNDIKSISEWCDQISVLYCGQ 236
Cdd:cd03269 146 DPELLILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
3-241 |
3.81e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 79.44 E-value: 3.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 3 LLDICNLNIEIQTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAikenwiitaDRFRFHDVELLKLSPHK 82
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGL---------DDGSSGEVSLVGQPLHQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 83 -----RRKIVGKEISMIFQNPLscLDPSrkigkqlIQNIPNWTFKNKWWKWFGWKKR-RAIELLHRVGIKDHRDIMasyP 156
Cdd:PRK10584 77 mdeeaRAKLRAKHVGFVFQSFM--LIPT-------LNALENVELPALLRGESSRQSRnGAKALLEQLGLGKRLDHL---P 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 157 NELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKsISEWCDQISVLYCGQ 236
Cdd:PRK10584 145 AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQ-LAARCDRRLRLVNGQ 223
|
....*
gi 1403710885 237 NTESA 241
Cdd:PRK10584 224 LQEEA 228
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-218 |
1.38e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 80.92 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 2 ALLDICNLNIEIQTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKEnwiiTADRFRFHDVELLKLSPH 81
Cdd:PRK10535 3 ALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKP----TSGTYRVAGQDVATLDAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 82 KRRKIVGKEISMIFQ--NPLSCLDPSRKIgkqliqNIPnwtfKNKWWKWFGWKKRRAIELLHRVGIKDHRDImasYPNEL 159
Cdd:PRK10535 79 ALAQLRREHFGFIFQryHLLSHLTAAQNV------EVP----AVYAGLERKQRLLRAQELLQRLGLEDRVEY---QPSQL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1403710885 160 TEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQnQGTTILLTSND 218
Cdd:PRK10535 146 SGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRD-RGHTVIIVTHD 203
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
26-254 |
1.74e-16 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 79.39 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 26 VNLSLNEGEITGLVGESGSGKSLIAKVICNAIK--ENWIITADRFRFHDVELLKLSPHKRRkivgkeISMIFQNplSCLD 103
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRpdEGEIVLNGRTLFDSRKGIFLPPEKRR------IGYVFQE--ARLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 104 PSRKIGKQLiqnipNWTFKNKWWKWFGWKKRRAIELLhrvGIkDHrdIMASYPNELTEGEGQKVMIAMAVANQPRLLIAD 183
Cdd:TIGR02142 88 PHLSVRGNL-----RYGMKRARPSERRISFERVIELL---GI-GH--LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1403710885 184 EPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCGQNTESAPTEILIESPHHPY 254
Cdd:TIGR02142 157 EPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
18-236 |
2.40e-16 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 76.91 E-value: 2.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 18 GRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKenwiITADRFRFHDVELLKLSPHKRrkivgkEISMIFQN 97
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEE----PTSGRIYIGGRDVTDLPPKDR------DIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 98 ---------------PLScldpSRKIGKQLIqnipnwtfknkwwkwfGWKKRRAIELLHRVGIKDHrdimasYPNELTEG 162
Cdd:cd03301 81 yalyphmtvydniafGLK----LRKVPKDEI----------------DERVREVAELLQIEHLLDR------KPKQLSGG 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1403710885 163 EGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCGQ 236
Cdd:cd03301 135 QRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQ 208
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-235 |
2.94e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 76.54 E-value: 2.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 21 KIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKENwiITADRFRFHDVELlklsphkrrkivGKEISmifqnpls 100
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGT--PVAGCVDVPDNQF------------GREAS-------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 101 cldpsrkigkqLIQNIP-NWTFKNkwwkwfgwkkrrAIELLHRVGIKDHRDIMASYPnELTEGEGQKVMIAMAVANQPRL 179
Cdd:COG2401 102 -----------LIDAIGrKGDFKD------------AVELLNAVGLSDAVLWLRRFK-ELSTGQKFRFRLALLLAERPKL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1403710885 180 LIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDiKSISEWCDQISVLYCG 235
Cdd:COG2401 158 LVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHH-YDVIDDLQPDLLIFVG 212
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
18-246 |
3.97e-16 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 76.32 E-value: 3.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 18 GRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKenwiITADRFRFHDVELLKLSPHKR-RKIVG--KEISMI 94
Cdd:cd03224 11 GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP----PRSGSIRFDGRDITGLPPHERaRAGIGyvPEGRRI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 95 FQNpLSCLD----PSRKIGKQLIQNIPNWTFknkwwkwfgwkkrraiELLHRvgIKDHRDIMASypnELTEGEGQKVMIA 170
Cdd:cd03224 87 FPE-LTVEEnlllGAYARRRAKRKARLERVY----------------ELFPR--LKERRKQLAG---TLSGGEQQMLAIA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1403710885 171 MAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQnQGTTILLTSNDIKSISEWCDQISVLYCGQNTESAPTEIL 246
Cdd:cd03224 145 RALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRD-EGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-260 |
1.41e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 75.17 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 1 MALLDICNLnieIQTSNGRiKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVIcNAIKENwiiTADRFRFHDVEL---LK 77
Cdd:PRK11264 1 MSAIEVKNL---VKKFHGQ-TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI-NLLEQP---EAGTIRVGDITIdtaRS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 78 LSPHKRR-KIVGKEISMIFQNplSCLDPSRKIGKQLIQNiPnwtfKNKWWKWFGWKKRRAIELLHRVGIKDHRDimaSYP 156
Cdd:PRK11264 73 LSQQKGLiRQLRQHVGFVFQN--FNLFPHRTVLENIIEG-P----VIVKGEPKEEATARARELLAKVGLAGKET---SYP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 157 NELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLT-----SNDIKSISEWCDQisv 231
Cdd:PRK11264 143 RRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVThemsfARDVADRAIFMDQ--- 219
|
250 260
....*....|....*....|....*....
gi 1403710885 232 lycGQNTESAPTEILIESPHHPYTQALIN 260
Cdd:PRK11264 220 ---GRIVEQGPAKALFADPQQPRTRQFLE 245
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
21-236 |
1.48e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 75.43 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 21 KIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNaikenwIITADRFRFHDVELLKLSPHKRRKIVGK------EISMI 94
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSG------LITGDKSAGSHIELLGRTVQREGRLARDirksraNTGYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 95 FQ-----NPLSCLDpSRKIGKqlIQNIPNWtfKNKWWKWFGWKKRRAIELLHRVGikdhrdiMASYPNE----LTEGEGQ 165
Cdd:PRK09984 92 FQqfnlvNRLSVLE-NVLIGA--LGSTPFW--RTCFSWFTREQKQRALQALTRVG-------MVHFAHQrvstLSGGQQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1403710885 166 KVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCGQ 236
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGH 230
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
17-214 |
2.00e-15 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 74.74 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 17 NGRiKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNaikENWIITADRFRFHDVELLKLSPHK-RRKI--VGKEISM 93
Cdd:COG1119 14 GGK-TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITG---DLPPTYGNDVRLFGERRGGEDVWElRKRIglVSPALQL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 94 IFQNPLSCLD-----------PSRKIGKQLIQnipnwtfknkwwkwfgwkkrRAIELLHRVGIKDHRDimASYpNELTEG 162
Cdd:COG1119 90 RFPRDETVLDvvlsgffdsigLYREPTDEQRE--------------------RARELLELLGLAHLAD--RPF-GTLSQG 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1403710885 163 EGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILL 214
Cdd:COG1119 147 EQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVL 198
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
12-249 |
7.10e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 73.51 E-value: 7.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 12 EIQTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKEnwiiTADRFRFHDVELLKLSPhkrrKIVGKEI 91
Cdd:PRK11231 7 NLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTP----QSGTVFLGDKPISMLSS----RQLARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 92 SMIFQNPLScldPSRKIGKQLIQ--NIPNWTFKNKWWKWFGWKKRRAIELLHRVGIKDHRdimasyPNELTEGEGQKVMI 169
Cdd:PRK11231 79 ALLPQHHLT---PEGITVRELVAygRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRR------LTDLSGGQRQRAFL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 170 AMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQnQGTTILLTSNDIKSISEWCDQISVLYCGQ-NTESAPTEILIE 248
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNT-QGKTVVTVLHDLNQASRYCDHLVVLANGHvMAQGTPEEVMTP 228
|
.
gi 1403710885 249 S 249
Cdd:PRK11231 229 G 229
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
26-248 |
1.11e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 73.23 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 26 VNLSLNEGEITGLVGESGSGKSLIAKVICNAIKEnwiiTADRFRFHDVELLKLSPHKRRKIVGKEISMIFQNPLSCLDpS 105
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQP----TEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLF-E 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 106 RKIGKQLIQNIPNWTFknkwwkWFGWKKRRAIELLHRVGIKdhRDIMASYPNELTEGEGQKVMIAMAVANQPRLLIADEP 185
Cdd:PRK13643 100 ETVLKDVAFGPQNFGI------PKEKAEKIAAEKLEMVGLA--DEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1403710885 186 TNALESTTALQVFRLLSSMNQNqGTTILLTSNDIKSISEWCDQISVLYCGQNTE-SAPTEILIE 248
Cdd:PRK13643 172 TAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIIScGTPSDVFQE 234
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
23-297 |
1.34e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 74.30 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 23 VDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKEnwiiTADRFRFHDVELLKLSPHKRRKIVGKEISMIFQNplSCL 102
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP----TRGQVLIDGVDIAKISDAELREVRRKKIAMVFQS--FAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 103 DPSRKIgkqliqnIPNWTFKNKWWKWFGWKKR-RAIELLHRVGIKDHRDimaSYPNELTEGEGQKVMIAMAVANQPRLLI 181
Cdd:PRK10070 118 MPHMTV-------LDNTAFGMELAGINAEERReKALDALRQVGLENYAH---SYPDELSGGMRQRVGLARALAINPDILL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 182 ADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCGQNTESAPTEILIESPHHPYTQALINA 261
Cdd:PRK10070 188 MDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRG 267
|
250 260 270
....*....|....*....|....*....|....*.
gi 1403710885 262 VpDFTQPlgFKTKLGTLEGTVPILEQMPigcRLGPR 297
Cdd:PRK10070 268 V-DISQV--FSAKDIARRTPNGLIRKTP---GFGPR 297
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
18-248 |
1.74e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.20 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 18 GRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKE-NW----IITADRFRFHDVellKLSPHKRRKIVGKEIS 92
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHgTYegeiIFEGEELQASNI---RDTERAGIAIIHQELA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 93 MIFQnpLSCLDpSRKIGKQLIQN-IPNWtfknkwwkwfGWKKRRAIELLHRVGIkdhrDIMASYP-NELTEGEGQKVMIA 170
Cdd:PRK13549 93 LVKE--LSVLE-NIFLGNEITPGgIMDY----------DAMYLRAQKLLAQLKL----DINPATPvGNLGLGQQQLVEIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 171 MAVANQPRLLIADEPTNAL---ESTTALQVFRLLssmnQNQGTTILLTSNDIKSISEWCDQISVLYCGQNTESAPTEILI 247
Cdd:PRK13549 156 KALNKQARLLILDEPTASLtesETAVLLDIIRDL----KAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMT 231
|
.
gi 1403710885 248 E 248
Cdd:PRK13549 232 E 232
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
13-232 |
3.04e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 73.67 E-value: 3.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 13 IQTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKEnwiiTADRFRFHDVELLKLSPHKRRK----IVG 88
Cdd:PRK09700 11 IGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEP----TKGTITINNINYNKLDHKLAAQlgigIIY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 89 KEISMIfqNPLSCLDpSRKIGKQLIQ-----NIPNWTFKNKwwkwfgwkkrRAIELLHRVGIKDHRDIMASypnELTEGE 163
Cdd:PRK09700 87 QELSVI--DELTVLE-NLYIGRHLTKkvcgvNIIDWREMRV----------RAAMMLLRVGLKVDLDEKVA---NLSISH 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1403710885 164 GQKVMIAMAVANQPRLLIADEPTNALestTALQVFRLLSSMNQ--NQGTTILLTSNDIKSISEWCDQISVL 232
Cdd:PRK09700 151 KQMLEIAKTLMLDAKVIIMDEPTSSL---TNKEVDYLFLIMNQlrKEGTAIVYISHKLAEIRRICDRYTVM 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
21-228 |
6.15e-14 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 72.53 E-value: 6.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 21 KIVDGVNLSLNEGEITGLVGESGSGKSLI--------------AKVI--------CNAIK------ENWIITADRFRFHD 72
Cdd:TIGR03269 14 EVLKNISFTIEEGEVLGILGRSGAGKSVLmhvlrgmdqyeptsGRIIyhvalcekCGYVErpskvgEPCPVCGGTLEPEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 73 VELLKLSPHKRRKIVgKEISMIFQNPLSCLDPSRKIgKQLIQNIPNWTFKNKWWKwfgwkkRRAIELLHRVGIkDHRdiM 152
Cdd:TIGR03269 94 VDFWNLSDKLRRRIR-KRIAIMLQRTFALYGDDTVL-DNVLEALEEIGYEGKEAV------GRAVDLIEMVQL-SHR--I 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1403710885 153 ASYPNELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQ 228
Cdd:TIGR03269 163 THIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDK 238
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-262 |
8.22e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 70.19 E-value: 8.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 2 ALLDICNLNIEIqtsnGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKenwiITADRFRFHDVELLKLSPH 81
Cdd:PRK13548 1 AMLEARNLSVRL----GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELS----PDSGEVRLNGRPLADWSPA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 82 ---KRRKIVGKEISMIFqnPLSCLD----------PSRKIGKQLIQnipnwtfknkwwkwfgwkkrraiELLHRVGIKD- 147
Cdd:PRK13548 73 elaRRRAVLPQHSSLSF--PFTVEEvvamgraphgLSRAEDDALVA-----------------------AALAQVDLAHl 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 148 -HRDimasYPnELTEGEGQKVMIAMAVA------NQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIK 220
Cdd:PRK13548 128 aGRD----YP-QLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLN 202
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1403710885 221 SISEWCDQISVLYCGQNT-ESAPTEILiesphhpyTQALINAV 262
Cdd:PRK13548 203 LAARYADRIVLLHQGRLVaDGTPAEVL--------TPETLRRV 237
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-259 |
9.21e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 70.46 E-value: 9.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 22 IVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIK--ENWIITADRFRFHDVELLKLSPHKRRkivgKEISMIFQNPl 99
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiyDSKIKVDGKVLYFGKDIFQIDAIKLR----KEVGMVFQQP- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 100 sclDPSRKIgkQLIQNIPnWTFKNKWWKWFGWKKRRAIELLHRVGI-KDHRDIMASYPNELTEGEGQKVMIAMAVANQPR 178
Cdd:PRK14246 100 ---NPFPHL--SIYDNIA-YPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLNSPASQLSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 179 LLIADEPTNALESTTALQVFRLLSSMNQNqgTTILLTSNDIKSISEWCDQISVLYCGQNTESAPTEILIESPHHPYTQAL 258
Cdd:PRK14246 174 VLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKY 251
|
.
gi 1403710885 259 I 259
Cdd:PRK14246 252 V 252
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
21-246 |
9.21e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 70.53 E-value: 9.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 21 KIVDGVNLSLNEGEITGLVGESGSGKSLIAkvicnaIKENWIITADRFRfhdVELLKLSPHKR-RKIVGKEISMIFQnpl 99
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLL------LHLNGIYLPQRGR---VKVMGREVNAEnEKWVRSKVGLVFQ--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 100 sclDPSRKIGKQLIQNipNWTF-KNKWWKWFGWKKRRAIELLHRVGIKDHRDimaSYPNELTEGEGQKVMIAMAVANQPR 178
Cdd:PRK13647 87 ---DPDDQVFSSTVWD--DVAFgPVNMGLDKDEVERRVEEALKAVRMWDFRD---KPPYHLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1403710885 179 LLIADEPTNALESTTALQVFRLLSSMNqNQGTTILLTSNDIKSISEWCDQISVLYCGQNTESAPTEIL 246
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLH-NQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLL 225
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
23-236 |
9.69e-14 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 68.61 E-value: 9.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 23 VDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKenwiITADRFRFHDVELLKLSPHKRRKivgkeismifqnplscl 102
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRP----PASGEITLDGKPVTRRSPRDAIR----------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 103 dpsRKIGkqliqNIPnwtfknkwwkwfgwkkrraiELLHRVGIKDHRDIM--ASYPNELTEGEGQKVMIAMAVANQPRLL 180
Cdd:cd03215 75 ---AGIA-----YVP--------------------EDRKREGLVLDLSVAenIALSSLLSGGNQQKVVLARWLARDPRVL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1403710885 181 IADEPTNALESTTALQVFRLLSSMNQnQGTTILLTSNDIKSISEWCDQISVLYCGQ 236
Cdd:cd03215 127 ILDEPTRGVDVGAKAEIYRLIRELAD-AGKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-232 |
9.88e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 70.89 E-value: 9.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 20 IKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNaikenwIITADRFRfhdVELLKLSPHKRRKIVGKEISMIFqnpl 99
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTG------ILVPTSGE---VRVLGYVPFKRRKEFARRIGVVF---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 100 scldpsrkiGK--QLIQNIPNW-TFKNKwwkwfgwkkrRAIellHRVGIKDHRDIMasypNELTE----GE--------- 163
Cdd:COG4586 102 ---------GQrsQLWWDLPAIdSFRLL----------KAI---YRIPDAEYKKRL----DELVElldlGElldtpvrql 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1403710885 164 --GQKvM---IAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVL 232
Cdd:COG4586 156 slGQR-MrceLAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVI 228
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
23-245 |
9.90e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 70.43 E-value: 9.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 23 VDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIK-ENWIITADRFrfhdvellKLSPHK----RRKivgkeISMIFQN 97
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLpEAGTITVGGM--------VLSEETvwdvRRQ-----VGMVFQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 98 PlscldpsrkiGKQLI--------------QNIPNwtfknkwwkwfGWKKRRAIELLHRVGIKD--HRDimasyPNELTE 161
Cdd:PRK13635 90 P----------DNQFVgatvqddvafglenIGVPR-----------EEMVERVDQALRQVGMEDflNRE-----PHRLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 162 GEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEwCDQISVLYCGQ-NTES 240
Cdd:PRK13635 144 GQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEiLEEG 222
|
....*
gi 1403710885 241 APTEI 245
Cdd:PRK13635 223 TPEEI 227
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
25-245 |
1.10e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 70.54 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 25 GVNLSLNEGEITGLVGESGSGKSLIAKVIcNAIKenwIITADRFRFHDVELLKLSPHKRRKIVGKEISMIFQNPLSCLDp 104
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLL-NGLH---VPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQFPESQLF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 105 SRKIGKQLI---QNIpnwtfknkwWKWFGWKKRRAIELLHRVGIKDhrDIMASYPNELTEGEGQKVMIAMAVANQPRLLI 181
Cdd:PRK13649 100 EETVLKDVAfgpQNF---------GVSQEEAEALAREKLALVGISE--SLFEKNPFELSGGQMRRVAIAGILAMEPKILV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1403710885 182 ADEPTNALESTTALQVFRLLSSMNQNqGTTILLTSNDIKSISEWCDQISVLYCGQNTESA-PTEI 245
Cdd:PRK13649 169 LDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGkPKDI 232
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
23-245 |
1.24e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 70.24 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 23 VDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKEnwiiTADRFRFHDVELLKLSPHKRRKIVGKEISMIFQNPLScl 102
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKP----SSGTITIAGYHITPETGNKNLKKLRKKVSLVFQFPEA-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 103 dpsrkigkQLIQNI---------PNWTFKNKWWKWfgwkkrRAIELLHRVGIKDhrDIMASYPNELTEGEGQKVMIAMAV 173
Cdd:PRK13641 97 --------QLFENTvlkdvefgpKNFGFSEDEAKE------KALKWLKKVGLSE--DLISKSPFELSGGQMRRVAIAGVM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1403710885 174 ANQPRLLIADEPTNALESTTALQVFRLLSSMnQNQGTTILLTSNDIKSISEWCDQISVLYCGQNTESA-PTEI 245
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHAsPKEI 232
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-249 |
1.42e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 70.12 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 3 LLDICNLNIEIQTSNGrIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKE-NWIITADRFRFHDVELLKLsph 81
Cdd:PRK13642 4 ILEVENLVFKYEKESD-VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEfEGKVKIDGELLTAENVWNL--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 82 kRRKivgkeISMIFQNPL-----SCLDPSRKIGKQlIQNIPNwtfknkwwkwfGWKKRRAIELLHRVGIKDHRdimASYP 156
Cdd:PRK13642 80 -RRK-----IGMVFQNPDnqfvgATVEDDVAFGME-NQGIPR-----------EEMIKRVDEALLAVNMLDFK---TREP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 157 NELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEwCDQISVLYCGQ 236
Cdd:PRK13642 139 ARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGE 217
|
250
....*....|....
gi 1403710885 237 -NTESAPTEILIES 249
Cdd:PRK13642 218 iIKEAAPSELFATS 231
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
18-262 |
2.08e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 69.18 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 18 GRIKIVDGVNLSLNEGEITGLVGESGSGKSliakVICNAIKENWIITADRFRFHD-----VELLKLSPHKRRKIVGKEIS 92
Cdd:PRK11701 17 GPRKGCRDVSFDLYPGEVLGIVGESGSGKT----TLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAERRRLLRTEWG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 93 MIFQNPLSCLDPS----RKIGKQLI-------QNIpnwtfknkwwkwfgwkKRRAIELLHRVGIKDHRdiMASYPNELTE 161
Cdd:PRK11701 93 FVHQHPRDGLRMQvsagGNIGERLMavgarhyGDI----------------RATAGDWLERVEIDAAR--IDDLPTTFSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 162 GEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCGQNTESA 241
Cdd:PRK11701 155 GMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
250 260
....*....|....*....|.
gi 1403710885 242 PTEILIESPHHPYTQALINAV 262
Cdd:PRK11701 235 LTDQVLDDPQHPYTQLLVSSV 255
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-232 |
2.15e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 69.75 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 18 GRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNaikenwIITAD----RFRFHdvellKLSPHKRRKI------V 87
Cdd:COG4152 12 GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILG------ILAPDsgevLWDGE-----PLDPEDRRRIgylpeeR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 88 GkeismifqnplscLDPSRKIGKQLI-----QNIPnwtfknkwwkwFGWKKRRAIELLHRVGIKDHRD--ImasypNELT 160
Cdd:COG4152 81 G-------------LYPKMKVGEQLVylarlKGLS-----------KAEAKRRADEWLERLGLGDRANkkV-----EELS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 161 EGEGQKVMIAMAVANQPRLLIADEP--------TNALESTtalqVFRLlssmnQNQGTTILLTSNDIKSISEWCDQISVL 232
Cdd:COG4152 132 KGNQQKVQLIAALLHDPELLILDEPfsgldpvnVELLKDV----IREL-----AAKGTTVIFSSHQMELVEELCDRIVII 202
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-256 |
2.15e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 69.30 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 21 KIVDGVNLSLNEGEITGLVGESGSGKSLIAKVIcNAIKEnwiITADRFRFHDVELLKLSPHKRRKIVG---KEISMIFQN 97
Cdd:PRK14258 21 KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNE---LESEVRVEGRVEFFNQNIYERRVNLNrlrRQVSMVHPK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 98 ----PLSCLDpSRKIGKQLIQNIPNWTFKNKWWKWFgwkkrRAIELLHRVGIKDHRDIMasypnELTEGEGQKVMIAMAV 173
Cdd:PRK14258 97 pnlfPMSVYD-NVAYGVKIVGWRPKLEIDDIVESAL-----KDADLWDEIKHKIHKSAL-----DLSGGQQQRLCIARAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 174 ANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLY-----CGQNTESAPTEILIE 248
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKgnenrIGQLVEFGLTKKIFN 245
|
....*...
gi 1403710885 249 SPHHPYTQ 256
Cdd:PRK14258 246 SPHDSRTR 253
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
12-236 |
2.72e-13 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 68.52 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 12 EIQTSN-----GRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKEnwiiTADRFRFHDVELLKLSPHKRrki 86
Cdd:cd03296 2 SIEVRNvskrfGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERP----DSGTILFGGEDATDVPVQER--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 87 vgkEISMIFQN-----PLSCLD----------PSRKIGKQLIQnipnwtfknkwwkwfgwkkRRAIELLHRVGIKDHRDi 151
Cdd:cd03296 75 ---NVGFVFQHyalfrHMTVFDnvafglrvkpRSERPPEAEIR-------------------AKVHELLKLVQLDWLAD- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 152 maSYPNELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISV 231
Cdd:cd03296 132 --RYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVV 209
|
....*
gi 1403710885 232 LYCGQ 236
Cdd:cd03296 210 MNKGR 214
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-250 |
3.69e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 69.87 E-value: 3.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 1 MALLDICNLNIEIqtsnGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKvicnAIKENWIITADRFRFHDVELLKLSP 80
Cdd:PRK09536 1 MPMIDVSDLSVEF----GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLR----AINGTLTPTAGTVLVAGDDVEALSA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 81 hkrrKIVGKEISMIFQNPLSCLDPSrkiGKQLIQ--NIPNWTFKNKWWKWFGWKKRRAIEllhRVGIkdhrDIMASYP-N 157
Cdd:PRK09536 73 ----RAASRRVASVPQDTSLSFEFD---VRQVVEmgRTPHRSRFDTWTETDRAAVERAME---RTGV----AQFADRPvT 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 158 ELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMnQNQGTTILLTSNDIKSISEWCDQISVLYCGQN 237
Cdd:PRK09536 139 SLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRL-VDDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
250
....*....|...
gi 1403710885 238 TESAPTEILIESP 250
Cdd:PRK09536 218 RAAGPPADVLTAD 230
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-256 |
4.52e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 68.33 E-value: 4.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 9 LNIEIQTSN-----GRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKENWIITAD---RFRFHDVELLKLSP 80
Cdd:PRK14267 1 MKFAIETVNlrvyyGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEgevRLFGRNIYSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 81 HKRRKIVGkeisMIFQ--NPLSCLdpsrkigkQLIQNIPNWTFKNKWWKWFGWKKRRAIELLHRVGIKDH-RDIMASYPN 157
Cdd:PRK14267 81 IEVRREVG----MVFQypNPFPHL--------TIYDNVAIGVKLNGLVKSKKELDERVEWALKKAALWDEvKDRLNDYPS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 158 ELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNqgTTILLTSNDIKSISEWCDQISVLYCGQN 237
Cdd:PRK14267 149 NLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
250
....*....|....*....
gi 1403710885 238 TESAPTEILIESPHHPYTQ 256
Cdd:PRK14267 227 IEVGPTRKVFENPEHELTE 245
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-246 |
8.82e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 67.23 E-value: 8.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 1 MALLDICNLnieIQTSNGRiKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAI-KENWIITADRfrfHDVELLKLS 79
Cdd:PRK10895 1 MATLTAKNL---AKAYKGR-RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVpRDAGNIIIDD---EDISLLPLH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 80 PHKRRKI--VGKEISM-----IFQNPLSCLDPSRKIGKQLIQNipnwtfknkwwkwfgwkkrRAIELLHRVGIKDHRDIM 152
Cdd:PRK10895 74 ARARRGIgyLPQEASIfrrlsVYDNLMAVLQIRDDLSAEQRED-------------------RANELMEEFHIEHLRDSM 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 153 AsypNELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMnQNQGTTILLTSNDIKSISEWCDQISVL 232
Cdd:PRK10895 135 G---QSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIV 210
|
250
....*....|....*
gi 1403710885 233 YCGQ-NTESAPTEIL 246
Cdd:PRK10895 211 SQGHlIAHGTPTEIL 225
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
24-245 |
1.16e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 67.41 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 24 DGVNLSLNEGEITGLVGESGSGKS---LIAKVICNAIKENWIITADRFRFHDVELLKLsphkrRKIVGkeisMIFQNPLS 100
Cdd:PRK13639 19 KGINFKAEKGEMVALLGPNGAGKStlfLHFNGILKPTSGEVLIKGEPIKYDKKSLLEV-----RKTVG----IVFQNPDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 101 CLDPSRKigKQLIQNIPnwtfkNKWWKWFGWKKRRAIELLHRVGIKDHRDimaSYPNELTEGEGQKVMIAMAVANQPRLL 180
Cdd:PRK13639 90 QLFAPTV--EEDVAFGP-----LNLGLSKEEVEKRVKEALKAVGMEGFEN---KPPHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1403710885 181 IADEPTNALESTTALQVFRLLSSMNQnQGTTILLTSNDIKSISEWCDQISVLYCGQ-NTESAPTEI 245
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLYDLNK-EGITIIISTHDVDLVPVYADKVYVMSDGKiIKEGTPKEV 224
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-255 |
1.62e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 67.04 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 22 IVDGVNLSLNEGEITGLVGESGSGKSLIAKVIcNAIKENwiITADRFRfHDVELLKLSPHKRRKIVG--KEISMIFQNP- 98
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTL-NRMNDK--VSGYRYS-GDVLLGGRSIFNYRDVLEfrRRVGMLFQRPn 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 99 ---LSCLDpSRKIGKQLIQNIPNWTFKNKwwkwfgwkkrrAIELLHRVGIKDH-RDIMASYPNELTEGEGQKVMIAMAVA 174
Cdd:PRK14271 112 pfpMSIMD-NVLAGVRAHKLVPRKEFRGV-----------AQARLTEVGLWDAvKDRLSDSPFRLSGGQQQLLCLARTLA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 175 NQPRLLIADEPTNALESTTALQVFRLLSSMNQNqgTTILLTSNDIKSISEWCDQISVLYCGQNTESAPTEILIESPHHPY 254
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAE 257
|
.
gi 1403710885 255 T 255
Cdd:PRK14271 258 T 258
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-248 |
2.85e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 67.54 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 18 GRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKENwiiTADRFRFHDVELLKLSphKRRKIVGKEISMIFQN 97
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHG---TWDGEIYWSGSPLKAS--NIRDTERAGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 98 PLSCLDPSrkigkqLIQNI--PNWTFKNKWWKWFGWKKRRAIELLHRVGIKDHRDimASYPNELTEGEGQKVMIAMAVAN 175
Cdd:TIGR02633 87 LTLVPELS------VAENIflGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNV--TRPVGDYGGGQQQLVEIAKALNK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1403710885 176 QPRLLIADEPTNAL---ESTTALQVFRLLssmnQNQGTTILLTSNDIKSISEWCDQISVLYCGQNTESAPTEILIE 248
Cdd:TIGR02633 159 QARLLILDEPSSSLtekETEILLDIIRDL----KAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSE 230
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
13-250 |
3.04e-12 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 65.26 E-value: 3.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 13 IQTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKENwiitADRFRFHDVELLKLSPHKR-RKIVG--- 88
Cdd:cd03218 6 LSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPD----SGKILLDGQDITKLPMHKRaRLGIGylp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 89 KEISmIF------QNPLSCLDPSRKIGKQLIQnipnwtfknkwwkwfgwkkrRAIELLHRVGIKDHRDIMASYpneLTEG 162
Cdd:cd03218 82 QEAS-IFrkltveENILAVLEIRGLSKKEREE--------------------KLEELLEEFHITHLRKSKASS---LSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 163 EGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNqNQGTTILLTSNDIKSISEWCDQISVLYCGQNTESAP 242
Cdd:cd03218 138 ERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILK-DRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGT 216
|
....*...
gi 1403710885 243 TEILIESP 250
Cdd:cd03218 217 PEEIAANE 224
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
18-235 |
4.37e-12 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 64.70 E-value: 4.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 18 GRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIK-ENWIITADRFRFHDvellklSPHKRRKIVGkeismIFQ 96
Cdd:cd03266 16 KTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEpDAGFATVDGFDVVK------EPAEARRRLG-----FVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 97 NPLSCLDpsRKIGKQLIQnipnwTFKNKWWKWFGWKKRRAIELLHRVGIKDHRDIMASypnELTEGEGQKVMIAMAVANQ 176
Cdd:cd03266 85 DSTGLYD--RLTARENLE-----YFAGLYGLKGDELTARLEELADRLGMEELLDRRVG---GFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1403710885 177 PRLLIADEPTNALE--STTAL-QVFRLLSSmnqnQGTTILLTSNDIKSISEWCDQISVLYCG 235
Cdd:cd03266 155 PPVLLLDEPTTGLDvmATRALrEFIRQLRA----LGKCILFSTHIMQEVERLCDRVVVLHRG 212
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
21-236 |
5.01e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 65.45 E-value: 5.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 21 KIVDGVNLSLNEGEITGLVGESGSGKS-LI-----------AKVICNAIKenwiITADRFRFHDVellklsphkrRKIVG 88
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKStLIqhlngllkptsGKIIIDGVD----ITDKKVKLSDI----------RKKVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 89 keisMIFQNPLSCL-----------DPSR-KIGKQLIQNipnwtfknkwwkwfgwKKRRAIELlhrVGIkDHRDIMASYP 156
Cdd:PRK13637 87 ----LVFQYPEYQLfeetiekdiafGPINlGLSEEEIEN----------------RVKRAMNI---VGL-DYEDYKDKSP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 157 NELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCGQ 236
Cdd:PRK13637 143 FELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
21-248 |
1.01e-11 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 63.79 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 21 KIVDGVNLSLNEGEITGLVGESGSGKSLIAKVIcnaikenwiitadrFRFHDVEllklspHKRRKIVGKEISMIFQNPLs 100
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLL--------------FRFYDVS------SGSILIDGQDIREVTLDSL- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 101 cldpSRKIG----------KQLIQNI----PNWTfknkwwkwfgwkkrrAIELLHRVGIKDHRDIMASYPN--------- 157
Cdd:cd03253 74 ----RRAIGvvpqdtvlfnDTIGYNIrygrPDAT---------------DEEVIEAAKAAQIHDKIMRFPDgydtivger 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 158 --ELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQgTTILLTSNdIKSISEwCDQISVLYCG 235
Cdd:cd03253 135 glKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGR-TTIVIAHR-LSTIVN-ADKIIVLKDG 211
|
250
....*....|...
gi 1403710885 236 QNTESAPTEILIE 248
Cdd:cd03253 212 RIVERGTHEELLA 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
18-185 |
1.43e-11 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 64.71 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 18 GRIKIVDGVNLSLNEGEITGLVGESGSGKS----LIA---KvicnaikenwiITADRFRFHDVELLKLSPHKRRkivgke 90
Cdd:COG3839 14 GGVEALKDIDLDIEDGEFLVLLGPSGCGKStllrMIAgleD-----------PTSGEILIGGRDVTDLPPKDRN------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 91 ISMIFQN---------------PLSCldpsRKIGKQLIQnipnwtfknkwwkwfgwkkRRAIELLHRVGIKDHRDimaSY 155
Cdd:COG3839 77 IAMVFQSyalyphmtvyeniafPLKL----RKVPKAEID-------------------RRVREAAELLGLEDLLD---RK 130
|
170 180 190
....*....|....*....|....*....|
gi 1403710885 156 PNELTEGEGQKVMIAMAVANQPRLLIADEP 185
Cdd:COG3839 131 PKQLSGGQRQRVALGRALVREPKVFLLDEP 160
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
12-218 |
2.31e-11 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 62.50 E-value: 2.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 12 EIQTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKENwiITAD-RFRFHDVELLKLSPHKRRkivgke 90
Cdd:COG4136 6 NLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPA--FSASgEVLLNGRRLTALPAEQRR------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 91 ISMIFQNPLscLDPSRKIGkqliQNIPnwtFKNKWWKWFGWKKRRAIELLHRVGIKD--HRDimasyPNELTEGEGQKVM 168
Cdd:COG4136 78 IGILFQDDL--LFPHLSVG----ENLA---FALPPTIGRAQRRARVEQALEEAGLAGfaDRD-----PATLSGGQRARVA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1403710885 169 IAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSND 218
Cdd:COG4136 144 LLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
9-243 |
2.32e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 63.95 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 9 LNIEIQTSN---GRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVIcnAIKENWiiTADRFRFHDVELLKLspHKRRK 85
Cdd:PRK10851 1 MSIEIANIKksfGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRII--AGLEHQ--TSGHIRFHGTDVSRL--HARDR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 86 IVGkeisMIFQN---------------PLSCLdPSRKigkqliqnIPNwtfknkwwkwFGWKKRRAIELLHRVGIkDHrd 150
Cdd:PRK10851 75 KVG----FVFQHyalfrhmtvfdniafGLTVL-PRRE--------RPN----------AAAIKAKVTQLLEMVQL-AH-- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 151 IMASYPNELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQIS 230
Cdd:PRK10851 129 LADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVV 208
|
250
....*....|...
gi 1403710885 231 VLYCGqNTESAPT 243
Cdd:PRK10851 209 VMSQG-NIEQAGT 220
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
28-222 |
2.91e-11 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 62.13 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 28 LSLNEGEITGLVGESGSGKSliakVICNAIKENWIITADRFRFHDVELLKLSPHKRrkivgkEISMIFQ--NPLSCLDPS 105
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKS----TLLNLIAGFETPQSGRVLINGVDVTAAPPADR------PVSMLFQenNLFAHLTVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 106 RKIGKQLIQNIpnwtfknkwwkWFGWKKRRAIE-LLHRVGIKdhrDIMASYPNELTEGEGQKVMIAMAVANQPRLLIADE 184
Cdd:cd03298 89 QNVGLGLSPGL-----------KLTAEDRQAIEvALARVGLA---GLEKRLPGELSGGERQRVALARVLVRDKPVLLLDE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1403710885 185 PTNALESTTALQVFRLLSSMNQNQGTTILLTSN---DIKSI 222
Cdd:cd03298 155 PFAALDPALRAEMLDLVLDLHAETKMTVLMVTHqpeDAKRL 195
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
22-245 |
3.11e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 63.28 E-value: 3.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 22 IVDGVNLSLNEGEITGLVGESGSGKSLIAKVIcNAI-----KENWIITADrfrfhDVELLKLSPHKRRKIVGkeisMIFQ 96
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLI-NGLllpddNPNSKITVD-----GITLTAKTVWDIREKVG----IVFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 97 NP------LSCLD------PSRKIGKQLIQNIPNwtfknkwwkwfgwkkrraiELLHRVGIKDHRDimaSYPNELTEGEG 164
Cdd:PRK13640 92 NPdnqfvgATVGDdvafglENRAVPRPEMIKIVR-------------------DVLADVGMLDYID---SEPANLSGGQK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 165 QKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSiSEWCDQISVLYCGQN-TESAPT 243
Cdd:PRK13640 150 QRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDE-ANMADQVLVLDDGKLlAQGSPV 228
|
..
gi 1403710885 244 EI 245
Cdd:PRK13640 229 EI 230
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
24-244 |
3.30e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 64.28 E-value: 3.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 24 DGVNLSLNEGEITGLVGESGSGKSLIAKVICNaikenwIITAD--RFRFHDVELLKLSPHKRRKIvGkeISMIFQN---- 97
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYG------LYQPDsgEILIDGKPVRIRSPRDAIAL-G--IGMVHQHfmlv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 98 -PLSCLDpsrkigkqliqNI-----PNWTFKNKWwkwfgwkkRRAIELLhrvgikdhRDIMASY-----PN----ELTEG 162
Cdd:COG3845 93 pNLTVAE-----------NIvlglePTKGGRLDR--------KAARARI--------RELSERYgldvdPDakveDLSVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 163 EGQKVMIAMAVANQPRLLIADEPTNALestTALQVFRLLSSMNQ--NQGTTILLTSNDIKSISEWCDQISVLYCGQNTES 240
Cdd:COG3845 146 EQQRVEILKALYRGARILILDEPTAVL---TPQEADELFEILRRlaAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGT 222
|
....
gi 1403710885 241 APTE 244
Cdd:COG3845 223 VDTA 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
23-245 |
3.36e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 63.18 E-value: 3.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 23 VDGVNLSLNEGEITGLVGESGSGKSLIAKVIcNAI---KENWIItadrfrfhdVELLKLSPHKRRKIVGKEISMIFQNPl 99
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHM-NALlipSEGKVY---------VDGLDTSDEENLWDIRNKAGMVFQNP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 100 scldpsrkiGKQLIQNI--PNWTFKNKWWKWFGWKKR-RAIELLHRVGIKDHRDimaSYPNELTEGEGQKVMIAMAVANQ 176
Cdd:PRK13633 95 ---------DNQIVATIveEDVAFGPENLGIPPEEIReRVDESLKKVGMYEYRR---HAPHLLSGGQKQRVAIAGILAMR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 177 PRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEwCDQISVLYCGQNT-ESAPTEI 245
Cdd:PRK13633 163 PECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVmEGTPKEI 231
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
18-259 |
3.52e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 62.49 E-value: 3.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 18 GRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVI--CNAIKENWIIT-ADRFRFHDVellkLSPHKRRKIVGKEISMI 94
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEVTITgSIVYNGHNI----YSPRTDTVDLRKEIGMV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 95 FQNPlsclDP-SRKIGKQLIQNIpnwtfkNKWWKWFGWKKRRAIEL-LHRVGIKDH-RDIMASYPNELTEGEGQKVMIAM 171
Cdd:PRK14239 92 FQQP----NPfPMSIYENVVYGL------RLKGIKDKQVLDEAVEKsLKGASIWDEvKDRLHDSALGLSGGQQQRVCIAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 172 AVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQgtTILLTSNDIKSISEWCDQISVLYCGQNTESAPTEILIESPH 251
Cdd:PRK14239 162 VLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPK 239
|
....*...
gi 1403710885 252 HPYTQALI 259
Cdd:PRK14239 240 HKETEDYI 247
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
12-249 |
3.91e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.88 E-value: 3.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 12 EIQTSNGRIKIVDGVNLSL-----NEGEITGLVGESGSGKSLIAKVICNaikENWIITADRF-RFHDVELLklSPHKRRK 85
Cdd:PRK10938 3 SLQISQGTFRLSDTKTLQLpsltlNAGDSWAFVGANGSGKSALARALAG---ELPLLSGERQsQFSHITRL--SFEQLQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 86 IVGKEismiFQ-NPLSCLDPSR----KIGKQLIQNipnwtfknkwwkwFGWKKRRAIELLHRVGIKDHRDIMASYpneLT 160
Cdd:PRK10938 78 LVSDE----WQrNNTDMLSPGEddtgRTTAEIIQD-------------EVKDPARCEQLAQQFGITALLDRRFKY---LS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 161 EGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQnQGTTILLTSNDIKSISEWCDQISVLYCGQNTES 240
Cdd:PRK10938 138 TGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQ-SGITLVLVLNRFDEIPDFVQFAGVLADCTLAET 216
|
250
....*....|
gi 1403710885 241 APTE-ILIES 249
Cdd:PRK10938 217 GEREeILQQA 226
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
23-232 |
6.50e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 62.17 E-value: 6.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 23 VDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKEnwiiTADRFRFHDvellKLSPHKRRKIVG--KEISMIFQNPLS 100
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKP----SSGRILFDG----KPIDYSRKGLMKlrESVGMVFQDPDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 101 CLdpsrkIGKQLIQNIpnwTFKNKWWKWFGWKKRRAIE-LLHRVGIKDHRDimasYPNE-LTEGEGQKVMIAMAVANQPR 178
Cdd:PRK13636 94 QL-----FSASVYQDV---SFGAVNLKLPEDEVRKRVDnALKRTGIEHLKD----KPTHcLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1403710885 179 LLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVL 232
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVM 215
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
23-282 |
6.81e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 62.08 E-value: 6.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 23 VDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKenwiITADRFRFHDvelLKLSPHKRRKIvGKEISMIFQNPlscl 102
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEK----VKSGEIFYNN---QAITDDNFEKL-RKHIGIVFQNP---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 103 dpsrkiGKQLIQNIPNWTFK---NKWWKWFGWKKRRAIELLHRVGIKDHRDimaSYPNELTEGEGQKVMIAMAVANQPRL 179
Cdd:PRK13648 93 ------DNQFVGSIVKYDVAfglENHAVPYDEMHRRVSEALKQVDMLERAD---YEPNALSGGQKQRVAIAGVLALNPSV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 180 LIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEwCDQISVLYCGQ-NTESAPTEILIESphhpytQAL 258
Cdd:PRK13648 164 IILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTvYKEGTPTEIFDHA------EEL 236
|
250 260 270
....*....|....*....|....*....|
gi 1403710885 259 INAVPDF------TQPLGFKTKLGTLEGTV 282
Cdd:PRK13648 237 TRIGLDLpfpikiNQMLGHQTSFLTYEGLV 266
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
20-236 |
9.94e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 62.03 E-value: 9.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 20 IKIVDGVNLSLNEGEITGLVGESGSGKS-----LIAKVICNAIKENWIITADRFRFHDVELLK------LSPHKRRKI-- 86
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTtfiehLNALLLPDTGTIEWIFKDEKNKKKTKEKEKvleklvIQKTRFKKIkk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 87 ---VGKEISMIFQNPLSCLDPSrKIGKQLIqnipnwtF-KNKWWKWFGWKKRRAIELLHRVGIKDhrDIMASYPNELTEG 162
Cdd:PRK13651 100 ikeIRRRVGVVFQFAEYQLFEQ-TIEKDII-------FgPVSMGVSKEEAKKRAAKYIELVGLDE--SYLQRSPFELSGG 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1403710885 163 EGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNqGTTILLTSNDIKSISEWCDQISVLYCGQ 236
Cdd:PRK13651 170 QKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGK 242
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
17-232 |
1.07e-10 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 62.87 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 17 NGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICnaikenwiitadrfRFHDVE----LL------KLSPHKRRki 86
Cdd:COG1132 350 PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLL--------------RFYDPTsgriLIdgvdirDLTLESLR-- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 87 vgKEISMIFQNP------------LSCLDPSRKigkqliqnipnwtfknkwwkwfgwkkrRAIELLHRVGIkdHRDIMAs 154
Cdd:COG1132 414 --RQIGVVPQDTflfsgtirenirYGRPDATDE---------------------------EVEEAAKAAQA--HEFIEA- 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 155 YPN----ELTE-------GEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMnqNQGTTILLTSNDIKSIS 223
Cdd:COG1132 462 LPDgydtVVGErgvnlsgGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERL--MKGRTTIVIAHRLSTIR 539
|
....*....
gi 1403710885 224 EwCDQISVL 232
Cdd:COG1132 540 N-ADRILVL 547
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-248 |
1.57e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 59.85 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 4 LDICNLNIEIqtsNGRiKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVIcnAIKENWIITADRFRFHDVELLKLSPHKR 83
Cdd:cd03217 1 LEIKDLHVSV---GGK-EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTI--MGHPKYEVTEGEILFKGEDITDLPPEER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 84 RKivgKEISMIFQNPLScldpsrkigkqlIQNIPNWTFKnkwwkwfgwkkrraiellhrvgikdhRDImasypNE-LTEG 162
Cdd:cd03217 75 AR---LGIFLAFQYPPE------------IPGVKNADFL--------------------------RYV-----NEgFSGG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 163 EGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNqNQGTTILLTS------NDIKSisewcDQISVLYCGQ 236
Cdd:cd03217 109 EKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLR-EEGKSVLIIThyqrllDYIKP-----DRVHVLYDGR 182
|
250
....*....|..
gi 1403710885 237 NTESAPTEILIE 248
Cdd:cd03217 183 IVKSGDKELALE 194
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
20-240 |
1.87e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 61.73 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 20 IKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICN---------AIkenwIITADRFRFHDvelLKLSPHKRRKIVGKE 90
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGvyphgsyegEI----LFDGEVCRFKD---IRDSEALGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 91 ISMIfqnplscldPSRKIGkqliQNI-----------PNWTfknkwwkwfgWKKRRAIELLHRVGIKDHRDIMASypnEL 159
Cdd:NF040905 87 LALI---------PYLSIA----ENIflgnerakrgvIDWN----------ETNRRARELLAKVGLDESPDTLVT---DI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 160 TEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMnQNQGTTILLTSNDIKSISEWCDQISVLYCGQNTE 239
Cdd:NF040905 141 GVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
.
gi 1403710885 240 S 240
Cdd:NF040905 220 T 220
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
22-236 |
1.99e-10 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 60.18 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 22 IVDGVNLSLNEGEITGLVGESGSGKSliakvICNAIKENWIITADRFRFHDVELLKLSPHK--RRKivgkeISMIFQNPL 99
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKS-----TVVALLENFYQPQGGQVLLDGKPISQYEHKylHSK-----VSLVGQEPV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 100 SCldpSRKIGKQLIQNIPNWTFKNKWWKWFGWKKRRAIELLHR-----VGIKDhrdimasypNELTEGEGQKVMIAMAVA 174
Cdd:cd03248 99 LF---ARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASgydteVGEKG---------SQLSGGQKQRVAIARALI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1403710885 175 NQPRLLIADEPTNALESTTALQVFRLLSSMNQNQgtTILLTSNDIKSIsEWCDQISVLYCGQ 236
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTV-ERADQILVLDGGR 225
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
22-219 |
2.14e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 60.48 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 22 IVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIK-ENWIITADrfrfhdvellklspHKRRKIVGKEISMIFQNplS 100
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPyQHGSITLD--------------GKPVEGPGAERGVVFQN--E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 101 CLDPSRKI------GKQLiQNIPNwtfknkwwkwfGWKKRRAIELLHRVGIK--DHRdimasYPNELTEGEGQKVMIAMA 172
Cdd:PRK11248 80 GLLPWRNVqdnvafGLQL-AGVEK-----------MQRLEIAHQMLKKVGLEgaEKR-----YIWQLSGGQRQRVGIARA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1403710885 173 VANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDI 219
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
22-219 |
2.52e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 60.08 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 22 IVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKENwiitadrfrfhDVELLKLSP--HKRRKivgkEISMIFQNpl 99
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPS-----------AGELLAGTAplAEARE----DTRLMFQD-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 100 SCLDPSRKIgkqlIQNIP-----NWtfknkwwkwfgwkKRRAIELLHRVGIKDHrdiMASYPNELTEGEGQKVMIAMAVA 174
Cdd:PRK11247 90 ARLLPWKKV----IDNVGlglkgQW-------------RDAALQALAAVGLADR---ANEWPAALSGGQKQRVALARALI 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1403710885 175 NQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDI 219
Cdd:PRK11247 150 HRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDV 194
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
21-246 |
2.84e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 60.41 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 21 KIVDGVNLSLNEGEITGLVGESGSGKS--------LIAKVICNAIKENWIITADRFRFHDVELLKlsphkrrkivgKEIS 92
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKStmiqltngLIISETGQTIVGDYAIPANLKKIKEVKRLR-----------KEIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 93 MIFQNPlscldpsrkiGKQLIQNI--PNWTFKNKWWKWFGWKKRRAI-ELLHRVGIKdhRDIMASYPNELTEGEGQKVMI 169
Cdd:PRK13645 94 LVFQFP----------EYQLFQETieKDIAFGPVNLGENKQEAYKKVpELLKLVQLP--EDYVKRSPFELSGGQKRRVAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1403710885 170 AMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCGQNTE-SAPTEIL 246
Cdd:PRK13645 162 AGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISiGSPFEIF 239
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
26-215 |
4.35e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 59.26 E-value: 4.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 26 VNLSLNEGEITGLVGESGSGKSLIAKVIcNAIK----ENWIITADRFRF----HDVELLKLsphkRRKiVGkeisMIFQN 97
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVL-NLLEmprsGTLNIAGNHFDFsktpSDKAIREL----RRN-VG----MVFQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 98 ----------------PLSCLDPSRKIGKQliqnipnwtfknkwwkwfgwkkrRAIELLHRVGIKDHRDimaSYPNELTE 161
Cdd:PRK11124 91 ynlwphltvqqnlieaPCRVLGLSKDQALA-----------------------RAEKLLERLRLKPYAD---RFPLHLSG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1403710885 162 GEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLT 215
Cdd:PRK11124 145 GQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVT 198
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
26-189 |
4.88e-10 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 60.11 E-value: 4.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 26 VNLSLNEGEITGLVGESGSGK-SLIakvicNAI------KENWIITADRFRFHDVELLKLSPHKRRkivgkeISMIFQNP 98
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKtTLL-----RAIaglerpDSGRIRLGGEVLQDSARGIFLPPHRRR------IGYVFQEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 99 LscLDPSRKIGKQL---IQNIPnwtfknkwWKWFGWKKRRAIELLhrvGIkdhRDIMASYPNELTEGEGQKVMIAMAVAN 175
Cdd:COG4148 87 R--LFPHLSVRGNLlygRKRAP--------RAERRISFDEVVELL---GI---GHLLDRRPATLSGGERQRVAIGRALLS 150
|
170
....*....|....
gi 1403710885 176 QPRLLIADEPTNAL 189
Cdd:COG4148 151 SPRLLLMDEPLAAL 164
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-265 |
6.99e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 59.85 E-value: 6.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 3 LLDICNLNieiQTSNGRiKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKEnwiiTADRFRFHDVELLKLSPHK 82
Cdd:PRK11607 19 LLEIRNLT---KSFDGQ-HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQP----TAGQIMLDGVDLSHVPPYQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 83 RrkivgkEISMIFQNplSCLDPSRKIGkqliQNIpnwTFKNKWWKWFGWKKR-RAIELLHRVGIKDhrdIMASYPNELTE 161
Cdd:PRK11607 91 R------PINMMFQS--YALFPHMTVE----QNI---AFGLKQDKLPKAEIAsRVNEMLGLVHMQE---FAKRKPHQLSG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 162 GEGQKVMIAMAVANQPRLLIADEPTNALEST----TALQVFRLLSSMnqnqGTTILLTSNDIKSISEWCDQISVLYCGQN 237
Cdd:PRK11607 153 GQRQRVALARSLAKRPKLLLLDEPMGALDKKlrdrMQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKF 228
|
250 260
....*....|....*....|....*...
gi 1403710885 238 TESAPTEILIESPHHPYTQALINAVPDF 265
Cdd:PRK11607 229 VQIGEPEEIYEHPTTRYSAEFIGSVNVF 256
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
136-250 |
7.93e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 58.65 E-value: 7.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 136 AIELlhrVGIKD--HRDImasypNELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTIL 213
Cdd:PRK10575 131 AISL---VGLKPlaHRLV-----DSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVI 202
|
90 100 110
....*....|....*....|....*....|....*..
gi 1403710885 214 LTSNDIKSISEWCDQISVLYCGQNTESAPTEILIESP 250
Cdd:PRK10575 203 AVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-244 |
9.87e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.68 E-value: 9.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 3 LLDICNlnieIQTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNaikenwIITAD--RFRFHDVELLKLSP 80
Cdd:PRK15439 11 LLCARS----ISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAG------IVPPDsgTLEIGGNPCARLTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 81 HKRRKIvgkEISMIFQNPLscLDPSRKIGKQLIQNIPNwtfknkwwkwFGWKKRRAIELLHRVGIKDHRDIMASypnELT 160
Cdd:PRK15439 81 AKAHQL---GIYLVPQEPL--LFPNLSVKENILFGLPK----------RQASMQKMKQLLAALGCQLDLDSSAG---SLE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 161 EGEGQKVMIAMAVANQPRLLIADEPTNALestTALQVFRLLSSMN--QNQGTTILLTSNDIKSISEWCDQISVLYCGQNT 238
Cdd:PRK15439 143 VADRQIVEILRGLMRDSRILILDEPTASL---TPAETERLFSRIRelLAQGVGIVFISHKLPEIRQLADRISVMRDGTIA 219
|
....*.
gi 1403710885 239 ESAPTE 244
Cdd:PRK15439 220 LSGKTA 225
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
26-244 |
1.07e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.68 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 26 VNLSLNEGEITGLVGESGSGKSLIAKVICNAIKENwiitADRFRFHDVELLKLSPHKR--RKIV----GKEISMIFqnpl 99
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPAR----GGRIMLNGKEINALSTAQRlaRGLVylpeDRQSSGLY---- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 100 scLDPSrkigkqLIQNIPNWTFKNKWWKWFGWKKRRAIELLHR-VGIK-DHRDIMAsypNELTEGEGQKVMIAMAVANQP 177
Cdd:PRK15439 354 --LDAP------LAWNVCALTHNRRGFWIKPARENAVLERYRRaLNIKfNHAEQAA---RTLSGGNQQKVLIAKCLEASP 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1403710885 178 RLLIADEPTNALESTTALQVFRLLSSMNQnQGTTILLTSNDIKSISEWCDQISVLYCGQNTESAPTE 244
Cdd:PRK15439 423 QLLIVDEPTRGVDVSARNDIYQLIRSIAA-QNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGA 488
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
3-99 |
1.15e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.11 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 3 LLDICNLNIEIqtsnGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVIcnAIKENWIITADRFRFHDVELLKLSPHK 82
Cdd:CHL00131 7 ILEIKNLHASV----NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVI--AGHPAYKILEGDILFKGESILDLEPEE 80
|
90
....*....|....*..
gi 1403710885 83 RRKivgKEISMIFQNPL 99
Cdd:CHL00131 81 RAH---LGIFLAFQYPI 94
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
162-235 |
1.30e-09 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 57.18 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 162 GEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQnQGTTILLT----SNdikSISEWCDQISVL----- 232
Cdd:cd03213 115 GERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAD-TGRTIICSihqpSS---EIFELFDKLLLLsqgrv 190
|
....
gi 1403710885 233 -YCG 235
Cdd:cd03213 191 iYFG 194
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
22-249 |
1.52e-09 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 57.50 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 22 IVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNA-IKENWIITADRfrfHDVELLKLSPHKRRKIVGKEISMIFqnpls 100
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyVPENGRVLVDG---HDLALADPAWLRRQVGVVLQENVLF----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 101 cldpSRKIgkqlIQNIpnwtfknkWWKWFGWKKRRAIELLHRVGIKD--------HRDIMASYPNELTEGEGQKVMIAMA 172
Cdd:cd03252 89 ----NRSI----RDNI--------ALADPGMSMERVIEAAKLAGAHDfiselpegYDTIVGEQGAGLSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 173 VANQPRLLIADEPTNAL--ESTTALQvfrllSSMNQ-NQGTTILLTSNDIKSISEwCDQISVLYCGQNTESAPTEILIES 249
Cdd:cd03252 153 LIHNPRILIFDEATSALdyESEHAIM-----RNMHDiCAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
10-236 |
1.86e-09 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 56.07 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 10 NIEIQTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNaikeNWIITADRFRFHDVELLKLSPHKRRKIVGk 89
Cdd:cd03246 5 NVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILG----LLRPTSGRVRLDGADISQWDPNELGDHVG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 90 eismifqnplscldpsrkigkQLIQNipnwtfknkwwkwfgwkkrraIELLHrvG-IKDhrdimasypNELTEGEGQKVM 168
Cdd:cd03246 80 ---------------------YLPQD---------------------DELFS--GsIAE---------NILSGGQRQRLG 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1403710885 169 IAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNdiKSISEWCDQISVLYCGQ 236
Cdd:cd03246 107 LARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHR--PETLASADRILVLEDGR 172
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-244 |
2.39e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 58.50 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 3 LLDICNLNIeiqTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKenwiITADRFRFHDVELLKLSPHK 82
Cdd:COG3845 257 VLEVENLSV---RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRP----PASGSIRLDGEDITGLSPRE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 83 RRK--------------IVGkeiSM-IFQNPLSCLDPSRKIGKQLIQNipnwtfknkwwkwfgwkkRRAIEllhrvgiKD 147
Cdd:COG3845 330 RRRlgvayipedrlgrgLVP---DMsVAENLILGRYRRPPFSRGGFLD------------------RKAIR-------AF 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 148 HRDIMASY----PNELTE------GEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMnQNQGTTILLTSN 217
Cdd:COG3845 382 AEELIEEFdvrtPGPDTParslsgGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISE 460
|
250 260
....*....|....*....|....*..
gi 1403710885 218 DIKSISEWCDQISVLYCGQNTESAPTE 244
Cdd:COG3845 461 DLDEILALSDRIAVMYEGRIVGEVPAA 487
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-217 |
3.35e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 57.02 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 21 KIVDGVNLSLNEGE-ITgLVGESGSGKS-LIakvicNAIKENWIITADRFRFHDVELLKLSPHKRRKIVGKeismIFQNP 98
Cdd:COG1101 20 RALDGLNLTIEEGDfVT-VIGSNGAGKStLL-----NAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGR----VFQDP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 99 LSCLDPSRKI----------GKqliqnipNWTFKNKWWKWFGWKKRRAIELLHRvGIKDHRDIMASYpneLTEGEGQKVM 168
Cdd:COG1101 90 MMGTAPSMTIeenlalayrrGK-------RRGLRRGLTKKRRELFRELLATLGL-GLENRLDTKVGL---LSGGQRQALS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1403710885 169 IAMAVANQPRLLIADEPTNALESTTALQVFRLLSSM-NQNQGTTILLTSN 217
Cdd:COG1101 159 LLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHN 208
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
22-243 |
4.57e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 56.66 E-value: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 22 IVDGVNLSLNEGEITGLVGESGSGKSLIAKVI---CNAIKENWIITADRFRFHDVEllklspHKRRKIvgkeiSMIFQNP 98
Cdd:PRK13650 22 TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIdglLEAESGQIIIDGDLLTEENVW------DIRHKI-----GMVFQNP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 99 lscldPSRKIGKQLIQNIpnwTFKNKWWKWFGWKKR-RAIELLHRVGIKDHRDimaSYPNELTEGEGQKVMIAMAVANQP 177
Cdd:PRK13650 91 -----DNQFVGATVEDDV---AFGLENKGIPHEEMKeRVNEALELVGMQDFKE---REPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1403710885 178 RLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISeWCDQISVLYCGQnTESAPT 243
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQ-VESTST 223
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
7-238 |
6.05e-09 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 54.94 E-value: 6.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 7 CNLNIEIQTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAiKENWIITADRFrfhdvellklsphkrrkI 86
Cdd:cd03232 7 KNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGR-KTAGVITGEIL-----------------I 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 87 VGKEISMIFQnplscldpsRKIG--KQLIQNIPNWTfknkwwkwfgwkKRRAIELlhrvgikdhrdimASYPNELTEGEG 164
Cdd:cd03232 69 NGRPLDKNFQ---------RSTGyvEQQDVHSPNLT------------VREALRF-------------SALLRGLSVEQR 114
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1403710885 165 QKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMnQNQGTTILLT-SNDIKSISEWCDQISVLYCGQNT 238
Cdd:cd03232 115 KRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKL-ADSGQAILCTiHQPSASIFEKFDRLLLLKRGGKT 188
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
18-248 |
1.33e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 54.99 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 18 GRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVIcnaikENWIITADRFRFHDVELLKlspHKRRKIVGKEISMIFQN 97
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTL-----SRLMTPAHGHVWLDGEHIQ---HYASKEVARRIGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 98 PLSCLDPSRK--IGKQLIQNIPNWTFKNKWWKWFGWKKRRAiellhrVGIKDhrdIMASYPNELTEGEGQKVMIAMAVAN 175
Cdd:PRK10253 90 ATTPGDITVQelVARGRYPHQPLFTRWRKEDEEAVTKAMQA------TGITH---LADQSVDTLSGGQRQRAWIAMVLAQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1403710885 176 QPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCGQ-NTESAPTEI----LIE 248
Cdd:PRK10253 161 ETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKiVAQGAPKEIvtaeLIE 238
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
12-236 |
1.35e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 54.89 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 12 EIQTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKEnwiiTADRFRFHDvellklsphkrRKIVGKEI 91
Cdd:PRK11614 10 KVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRA----TSGRIVFDG-----------KDITDWQT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 92 SMIFQNPLSCLDPSRKIGKQLI--QNIPNWTFKNKWWKWFGWKkRRAIELLHRVGIKDHRDimasyPNELTEGEGQKVMI 169
Cdd:PRK11614 75 AKIMREAVAIVPEGRRVFSRMTveENLAMGGFFAERDQFQERI-KWVYELFPRLHERRIQR-----AGTMSGGEQQMLAI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1403710885 170 AMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQnQGTTILLTSNDIKSISEWCDQISVLYCGQ 236
Cdd:PRK11614 149 GRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLRE-QGMTIFLVEQNANQALKLADRGYVLENGH 214
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
21-202 |
1.61e-08 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 54.20 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 21 KIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKENWIITADRFrFHDVELlklSPHKRRKIVGkeismifqnpls 100
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQIL-FNGQPR---KPDQFQKCVA------------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 101 cldpsrkIGKQLIQNIPN------WTFKNKWWKWFGWKKRRAIELLHRVGIKD--HRDIMASYPNELTEGEGQKVMIAMA 172
Cdd:cd03234 85 -------YVRQDDILLPGltvretLTYTAILRLPRKSSDAIRKKRVEDVLLRDlaLTRIGGNLVKGISGGERRRVSIAVQ 157
|
170 180 190
....*....|....*....|....*....|
gi 1403710885 173 VANQPRLLIADEPTNALESTTALQVFRLLS 202
Cdd:cd03234 158 LLWDPKVLILDEPTSGLDSFTALNLVSTLS 187
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
13-248 |
1.66e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 55.22 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 13 IQTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNaikenwIITADRfrfHDVELLKLSPHKRRKIVGKEIS 92
Cdd:PRK13536 47 VSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILG------MTSPDA---GKITVLGVPVPARARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 93 MIFQnpLSCLDPSRKIGKQLIqnIPNWTFKNKWwkwfgwkkrRAIE-----LLHRVGIKDHRDIMASypnELTEGEGQKV 167
Cdd:PRK13536 118 VVPQ--FDNLDLEFTVRENLL--VFGRYFGMST---------REIEavipsLLEFARLESKADARVS---DLSGGMKRRL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 168 MIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMnQNQGTTILLTSNDIKSISEWCDQISVLYCGQN-TESAPTEIL 246
Cdd:PRK13536 182 TLARALINDPQLLILDEPTTGLDPHARHLIWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVLEAGRKiAEGRPHALI 260
|
..
gi 1403710885 247 IE 248
Cdd:PRK13536 261 DE 262
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-219 |
1.72e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 54.77 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 3 LLDICNLNIeiqtSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIK----ENW-----IITADRFRFHDV 73
Cdd:PRK11831 7 LVDMRGVSF----TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIApdhgEILfdgenIPAMSRSRLYTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 74 EllklsphkrrkivgKEISMIFQNPLSCLDPSrkigkqLIQNIPnWTFKNKWWKWFGWKKRRAIELLHRVGIKDHRDIMa 153
Cdd:PRK11831 83 R--------------KRMSMLFQSGALFTDMN------VFDNVA-YPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLM- 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1403710885 154 syPNELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDI 219
Cdd:PRK11831 141 --PSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDV 204
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-99 |
1.89e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 54.41 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 3 LLDICNLNIEIQTSngriKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVIcnAIKENWIITADRFRFHDVELLKLSPHK 82
Cdd:PRK09580 1 MLSIKDLHVSVEDK----AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATL--AGREDYEVTGGTVEFKGKDLLELSPED 74
|
90
....*....|....*..
gi 1403710885 83 RrkiVGKEISMIFQNPL 99
Cdd:PRK09580 75 R---AGEGIFMAFQYPV 88
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
14-236 |
3.84e-08 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 53.31 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 14 QTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNaikenwIITADRFRFhdvellklsphkrrKIVGKEISM 93
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAG------IYPPDSGTV--------------TVRGRVSSL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 94 I-----FQNPLSCLDPSRKIGkqLIQNIPNwtfknkwwkwfgwkkRRAIELLHRV----GIKDHRDI-MASYPNeltege 163
Cdd:cd03220 89 LglgggFNPELTGRENIYLNG--RLLGLSR---------------KEIDEKIDEIiefsELGDFIDLpVKTYSS------ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1403710885 164 GQKVMIAMAVAN--QPRLLIADEPTNALESTTALQVFRLLSSMnQNQGTTILLTSNDIKSISEWCDQISVLYCGQ 236
Cdd:cd03220 146 GMKARLAFAIATalEPDILLIDEVLAVGDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRLCDRALVLEKGK 219
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
22-249 |
3.92e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 54.04 E-value: 3.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 22 IVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKENwiitADRFRFHDVELLKLSPHKRRKiVGkeISMIFQNplsc 101
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPD----AGSISLCGEPVPSRARHARQR-VG--VVPQFDN---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 102 LDPSRKIGKQLIqnipnwTFKNKWWKWFGWKKRRAIELLHRVGIKDHRDIMASypnELTEGEGQKVMIAMAVANQPRLLI 181
Cdd:PRK13537 91 LDPDFTVRENLL------VFGRYFGLSAAAARALVPPLLEFAKLENKADAKVG---ELSGGMKRRLTLARALVNDPDVLV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1403710885 182 ADEPTNALESTTALQVFRLLSSMnQNQGTTILLTSNDIKSISEWCDQISVLYCGQN-TESAPTEiLIES 249
Cdd:PRK13537 162 LDEPTTGLDPQARHLMWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVIEEGRKiAEGAPHA-LIES 228
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
22-246 |
4.83e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 53.46 E-value: 4.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 22 IVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKEnwiiTADRFRFHDVELLKLSPHKRRKIVGkeisMIFQNPlsc 101
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKP----QSGEIKIDGITISKENLKEIRKKIG----IIFQNP--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 102 ldPSRKIGKQLIQNIpnwTFKNKWWKWFGWKKRRAI-ELLHRVGIKDHRDimaSYPNELTEGEGQKVMIAMAVANQPRLL 180
Cdd:PRK13632 93 --DNQFIGATVEDDI---AFGLENKKVPPKKMKDIIdDLAKKVGMEDYLD---KEPQNLSGGQKQRVAIASVLALNPEII 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1403710885 181 IADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEwCDQISVLYCGQNTESA-PTEIL 246
Cdd:PRK13632 165 IFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGkPKEIL 230
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
138-236 |
7.82e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 53.90 E-value: 7.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 138 ELLHRVGIKDHRDIMASYPNE---LTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNqGTTILL 214
Cdd:TIGR00955 143 EVLQALGLRKCANTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQK-GKTIIC 221
|
90 100
....*....|....*....|...
gi 1403710885 215 TSNDIKS-ISEWCDQISVLYCGQ 236
Cdd:TIGR00955 222 TIHQPSSeLFELFDKIILMAEGR 244
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-246 |
7.90e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 52.70 E-value: 7.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 21 KIVDGVNLSLNEGEITGLVGESGSGKSLIakvicnaikenWIITADRFRFHDVELL---KLSPHKRRKIVG--KEISMIF 95
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTL-----------FMNLSGLLRPQKGAVLwqgKPLDYSKRGLLAlrQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 96 QnplsclDPSRKIGKQLIQNIPNWTFKNKWWKWFGWKkRRAIELLHRVGIKDHRdimaSYPNE-LTEGEGQKVMIAMAVA 174
Cdd:PRK13638 84 Q------DPEQQIFYTDIDSDIAFSLRNLGVPEAEIT-RRVDEALTLVDAQHFR----HQPIQcLSHGQKKRVAIAGALV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1403710885 175 NQPRLLIADEPTNALESTTALQVFRLLSSMNQnQGTTILLTSNDIKSISEWCDQISVLYCGQN-TESAPTEIL 246
Cdd:PRK13638 153 LQARYLLLDEPTAGLDPAGRTQMIAIIRRIVA-QGNHVIISSHDIDLIYEISDAVYVLRQGQIlTHGAPGEVF 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-236 |
1.46e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.99 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 20 IKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNaikeNWIITADRFRfhdvellklsphkrrkIVGKEisMIFQNPL 99
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSG----NYQPDAGSIL----------------IDGQE--MRFASTT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 100 SCLDPSRKIGKQLIQNIPNWTF----------KNKWWKWFGWKKRRAIELLHRVGIkdhrDIMASYP-NELTEGEGQKVM 168
Cdd:PRK11288 75 AALAAGVAIIYQELHLVPEMTVaenlylgqlpHKGGIVNRRLLNYEAREQLEHLGV----DIDPDTPlKYLSIGQRQMVE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1403710885 169 IAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMnQNQGTTILLTSNDIKSISEWCDQISVLYCGQ 236
Cdd:PRK11288 151 IAKALARNARVIAFDEPTSSLSAREIEQLFRVIREL-RAEGRVILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
10-213 |
1.77e-07 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 52.89 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 10 NIEIQTSNGRIkIVDGVNLSLNEGEITGLVGESGSGKSLiakvicnaikenwiitadrfrfhdveLLK----LSPHKRRK 85
Cdd:COG4178 367 DLTLRTPDGRP-LLEDLSLSLKPGERLLITGPSGSGKST--------------------------LLRaiagLWPYGSGR 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 86 IV---GKEISMIFQN---PLSCL-------DPSRKIGKQliqnipnwtfknkwwkwfgwkkrRAIELLHRVG---IKDHR 149
Cdd:COG4178 420 IArpaGARVLFLPQRpylPLGTLreallypATAEAFSDA-----------------------ELREALEAVGlghLAERL 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1403710885 150 DIMASYPNELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSmnQNQGTTIL 213
Cdd:COG4178 477 DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVI 538
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
23-233 |
1.85e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 52.71 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 23 VDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKenwiITADRFRFHDVELLKLSPHKR-----------RKIVGkei 91
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADP----ADSGEIRLDGKPVRIRSPRDAiragiayvpedRKGEG--- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 92 smIFQNpLSCLDpsrkigkqliqNI--PNW-TFKNKWWKWFGWKKRRAIELLHRVGIKdhrdimASYPNELTE----GEG 164
Cdd:COG1129 341 --LVLD-LSIRE-----------NItlASLdRLSRGGLLDRRRERALAEEYIKRLRIK------TPSPEQPVGnlsgGNQ 400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1403710885 165 QKVMIAMAVANQPRLLIADEPT-----NALEsttalQVFRLLSSMNQnQGTTILLTSNDIKSISEWCDQISVLY 233
Cdd:COG1129 401 QKVVLAKWLATDPKVLILDEPTrgidvGAKA-----EIYRLIRELAA-EGKAVIVISSELPELLGLSDRILVMR 468
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
8-259 |
2.63e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 51.32 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 8 NLNIEIQTSN-----GRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKviC----NAIKENWIITADRFrFHDVELLkl 78
Cdd:PRK14243 6 GTETVLRTENlnvyyGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILR--CfnrlNDLIPGFRVEGKVT-FHGKNLY-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 79 SPHKRRKIVGKEISMIFQNPlsclDPsrkIGKQLIQNIPNWTFKNKWWKWFGWKKRRAielLHRVGIKDH-RDIMASYPN 157
Cdd:PRK14243 81 APDVDPVEVRRRIGMVFQKP----NP---FPKSIYDNIAYGARINGYKGDMDELVERS---LRQAALWDEvKDKLKQSGL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 158 ELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQnQGTTILLTSNdIKSISEWCDQISVLYC--- 234
Cdd:PRK14243 151 SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKE-QYTIIIVTHN-MQQAARVSDMTAFFNVelt 228
|
250 260 270
....*....|....*....|....*....|.
gi 1403710885 235 ------GQNTESAPTEILIESPHHPYTQALI 259
Cdd:PRK14243 229 egggryGYLVEFDRTEKIFNSPQQQATRDYV 259
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
8-236 |
4.52e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 49.57 E-value: 4.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 8 NLNIEIQTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKENWIITADrFRFHDVELLKLSPHKRRkiv 87
Cdd:cd03233 8 NISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGD-IHYNGIPYKEFAEKYPG--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 88 gkEISMIFQNPLscldpsrkigkqliqNIPNWTfknkwwkwfgwkKRRAIELlhRVGIKDHRdimasYPNELTEGEGQKV 167
Cdd:cd03233 84 --EIIYVSEEDV---------------HFPTLT------------VRETLDF--ALRCKGNE-----FVRGISGGERKRV 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1403710885 168 MIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLT----SNDIKSIsewCDQISVLYCGQ 236
Cdd:cd03233 128 SIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSlyqaSDEIYDL---FDKVLVLYEGR 197
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
157-239 |
1.09e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.17 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 157 NELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMnQNQGTTILLTSNDIKSISEWCDQISVLYCGQ 236
Cdd:PRK09700 408 TELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGR 486
|
...
gi 1403710885 237 NTE 239
Cdd:PRK09700 487 LTQ 489
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
22-250 |
2.50e-06 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 49.34 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 22 IVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKEN-WIITADRFRFHDVELLKLspHKRRKIVGKEISM----IFQ 96
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTgGQVLLDGVPLVQYDHHYL--HRQVALVGQEPVLfsgsVRE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 97 NPLSCLDpsrKIGKQLIQNIPNWTFKnkwwkwfgwkkrraiellHRVGIKDHRDI---MASYPNELTEGEGQKVMIAMAV 173
Cdd:TIGR00958 574 NIAYGLT---DTPDEEIMAAAKAANA------------------HDFIMEFPNGYdteVGEKGSQLSGGQKQRIAIARAL 632
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1403710885 174 ANQPRLLIADEPTNALESttalQVFRLLSSMNQNQGTTILLTSNDIkSISEWCDQISVLYCGQNTESAPTEILIESP 250
Cdd:TIGR00958 633 VRKPRVLILDEATSALDA----ECEQLLQESRSRASRTVLLIAHRL-STVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
20-212 |
2.51e-06 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 48.00 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 20 IKIVDGVNLSLNEGEITGLVGESGSGKSliakVICNAIKENWIITADRFRF--HDVELLKLSPHKRrkivgkEISMIFQN 97
Cdd:cd03251 15 PPVLRDISLDIPAGETVALVGPSGSGKS----TLVNLIPRFYDVDSGRILIdgHDVRDYTLASLRR------QIGLVSQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 98 PLSCLDPSRkigkqliQNI----PNWTfknkwwkwfGWKKRRAIELLHRvgikdHRDIMaSYPN-----------ELTEG 162
Cdd:cd03251 85 VFLFNDTVA-------ENIaygrPGAT---------REEVEEAARAANA-----HEFIM-ELPEgydtvigergvKLSGG 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1403710885 163 EGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQgTTI 212
Cdd:cd03251 143 QRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNR-TTF 191
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-236 |
3.82e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 48.28 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 17 NGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKENW------------IITADRFRFHDVELLklsPHKRR 84
Cdd:TIGR02633 270 NPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFegnvfingkpvdIRNPAQAIRAGIAMV---PEDRK 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 85 K-------IVGKEISmifqnpLSCLDPSRKIGKqliqnipnwtfknKWWKWFGWKKRRAIELLHrvgikdhrdIMASYPN 157
Cdd:TIGR02633 347 RhgivpilGVGKNIT------LSVLKSFCFKMR-------------IDAAAELQIIGSAIQRLK---------VKTASPF 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 158 ----ELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQnQGTTILLTSNDIKSISEWCDQISVLY 233
Cdd:TIGR02633 399 lpigRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQ-EGVAIIVVSSELAEVLGLSDRVLVIG 477
|
...
gi 1403710885 234 CGQ 236
Cdd:TIGR02633 478 EGK 480
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
13-219 |
5.85e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 47.03 E-value: 5.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 13 IQTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKEnwiitadrfrfhDVELLKLSPHKRRKIVGKEIS 92
Cdd:PRK09544 10 VSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAP------------DEGVIKRNGKLRIGYVPQKLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 93 MIFQNPLSCldpsrkigKQLIQNIPNwtfknkwwkwfgwkKRRA--IELLHRVgikdHRDIMASYP-NELTEGEGQKVMI 169
Cdd:PRK09544 78 LDTTLPLTV--------NRFLRLRPG--------------TKKEdiLPALKRV----QAGHLIDAPmQKLSGGETQRVLL 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1403710885 170 AMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDI 219
Cdd:PRK09544 132 ARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
22-189 |
6.88e-06 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 47.25 E-value: 6.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 22 IVDGVNLSLNEGEITGLVGESGSGKSLIAKVIcnAIKENwiITADRFRFHDVELLKLSPHKRrkivgkEISMIFQNplSC 101
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLI--AGFET--PDSGRIMLDGQDITHVPAENR------HVNTVFQS--YA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 102 LDPSRKIGKQL-----IQNIPNwtfknkwwkwfGWKKRRAIELLHRVGIKDHRDimaSYPNELTEGEGQKVMIAMAVANQ 176
Cdd:PRK09452 97 LFPHMTVFENVafglrMQKTPA-----------AEITPRVMEALRMVQLEEFAQ---RKPHQLSGGQQQRVAIARAVVNK 162
|
170
....*....|...
gi 1403710885 177 PRLLIADEPTNAL 189
Cdd:PRK09452 163 PKVLLLDESLSAL 175
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
26-189 |
7.06e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 47.18 E-value: 7.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 26 VNLSLNEGEITGLVGESGSGK-SLIakvicNAI------KENWIITADRFRFHDVELLKLSPHKRRkivgkeISMIFQNp 98
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKtSLI-----NAIsgltrpQKGRIVLNGRVLFDAEKGICLPPEKRR------IGYVFQD- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 99 lSCLDPSRKIGKQL---IQNIPNWTFKnkwwkwfgwkkrRAIELLhrvGIKDHRDimaSYPNELTEGEGQKVMIAMAVAN 175
Cdd:PRK11144 85 -ARLFPHYKVRGNLrygMAKSMVAQFD------------KIVALL---GIEPLLD---RYPGSLSGGEKQRVAIGRALLT 145
|
170
....*....|....
gi 1403710885 176 QPRLLIADEPTNAL 189
Cdd:PRK11144 146 APELLLMDEPLASL 159
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
23-232 |
9.24e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 46.52 E-value: 9.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 23 VDGVNLSLNEGEITGLVGESGSGKSliakVICNAIKENWIITADRFRFHDVELLKLSPHKrrkIVGKEISMIFQNPlscl 102
Cdd:PRK11300 21 VNNVNLEVREQEIVSLIGPNGAGKT----TVFNCLTGFYKPTGGTILLRGQHIEGLPGHQ---IARMGVVRTFQHV---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 103 dpsrKIGKQL--IQNI-------------------PNWtfknkwWKWFGWKKRRAIELLHRVGIKDHRDIMASypnELTE 161
Cdd:PRK11300 90 ----RLFREMtvIENLlvaqhqqlktglfsgllktPAF------RRAESEALDRAATWLERVGLLEHANRQAG---NLAY 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1403710885 162 GEGQKVMIAMAVANQPRLLIADEPTNAL--ESTTALQvfRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVL 232
Cdd:PRK11300 157 GQQRRLEIARCMVTQPEILMLDEPAAGLnpKETKELD--ELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVV 227
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
22-213 |
2.78e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 46.03 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 22 IVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKEN----WIITADRfrfhdvellklsphKRRKIVGKEISMIFQN 97
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnftgTILANNR--------------KPTKQILKRTGFVTQD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 98 PLscLDPSRKIGKQLI----QNIPNwtfknkwWKWFGWKKRRAIELLHRVGIK--DHRDIMASYPNELTEGEGQKVMIAM 171
Cdd:PLN03211 149 DI--LYPHLTVRETLVfcslLRLPK-------SLTKQEKILVAESVISELGLTkcENTIIGNSFIRGISGGERKRVSIAH 219
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1403710885 172 AVANQPRLLIADEPTNALESTTALQVFRLLSSMNQnQGTTIL 213
Cdd:PLN03211 220 EMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQ-KGKTIV 260
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
20-196 |
2.90e-05 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 44.84 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 20 IKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVIcnaikenwiitadrFRFHD----------VELLKLSPHKRRK---I 86
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLL--------------ERFYDptsgeilldgVDIRDLNLRWLRSqigL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 87 VGKEiSMIFQNPLScldpsrkigkqliQNI----PNWTfknkwwkwfGWKKRRAIEL--LHrvgikdhrDIMASYPN--- 157
Cdd:cd03249 82 VSQE-PVLFDGTIA-------------ENIrygkPDAT---------DEEVEEAAKKanIH--------DFIMSLPDgyd 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1403710885 158 --------ELTEGEGQKVMIAMAVANQPRLLIADEPTNAL--ESTTALQ 196
Cdd:cd03249 131 tlvgergsQLSGGQKQRIAIARALLRNPKILLLDEATSALdaESEKLVQ 179
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
17-249 |
3.03e-05 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 44.52 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 17 NGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICnaikenwiitadrfRFHD----------VELLKLSphkrRKI 86
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLM--------------RFYDpqkgqilidgIDIRDIS----RKS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 87 VGKEISMIFQNPLSCldpSRKIGKQLIQNIPNWTfknkwwkwfgwkKRRAIELLHRVGIkdHRDIM------ASYPNE-- 158
Cdd:cd03254 75 LRSMIGVVLQDTFLF---SGTIMENIRLGRPNAT------------DEEVIEAAKEAGA--HDFIMklpngyDTVLGEng 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 159 --LTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQgTTILLTSNdiKSISEWCDQISVLYCGQ 236
Cdd:cd03254 138 gnLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGR-TSIIIAHR--LSTIKNADKILVLDDGK 214
|
250
....*....|...
gi 1403710885 237 NTESAPTEILIES 249
Cdd:cd03254 215 IIEEGTHDELLAK 227
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-232 |
4.44e-05 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 42.82 E-value: 4.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 4 LDICNLNIEIqtsNGRiKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKEnwiitadrfrfhdvellklsphkr 83
Cdd:cd03221 1 IELENLSKTY---GGK-LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEP------------------------ 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 84 rkIVGKeismifqnplscldpsrkigkqliqnipnwtfknkwwkwfgwkkrraiellhrvgIKDHRDIMASYPNELTEGE 163
Cdd:cd03221 53 --DEGI-------------------------------------------------------VTWGSTVKIGYFEQLSGGE 75
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1403710885 164 GQKVMIAMAVANQPRLLIADEPTNAL--ESTTALQVFrllssMNQNQGtTILLTSNDIKSISEWCDQISVL 232
Cdd:cd03221 76 KMRLALAKLLLENPNLLLLDEPTNHLdlESIEALEEA-----LKEYPG-TVILVSHDRYFLDQVATKIIEL 140
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
16-235 |
6.85e-05 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 44.25 E-value: 6.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 16 SNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVIcnAIKENwIITADRF----RFHDVEllklsPHKRrkivgkEI 91
Cdd:PRK11000 12 AYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMI--AGLED-ITSGDLFigekRMNDVP-----PAER------GV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 92 SMIFQN----P-LSCLDpsrkigkqliqnipNWTFKNKWWKWFGWKKRRAIELLHRVGIKDHrdIMASYPNELTEGEGQK 166
Cdd:PRK11000 78 GMVFQSyalyPhLSVAE--------------NMSFGLKLAGAKKEEINQRVNQVAEVLQLAH--LLDRKPKALSGGQRQR 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1403710885 167 VMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEWCDQISVLYCG 235
Cdd:PRK11000 142 VAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAG 210
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
134-235 |
9.21e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 44.35 E-value: 9.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 134 RRAIELLHRVGIKDHRDimaSYPNELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTIL 213
Cdd:NF033858 376 ARVAEMLERFDLADVAD---ALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIF 452
|
90 100 110
....*....|....*....|....*....|.
gi 1403710885 214 LTS---NDiksiSEWCDQIS------VLYCG 235
Cdd:NF033858 453 ISThfmNE----AERCDRISlmhagrVLASD 479
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
135-250 |
1.29e-04 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 42.76 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 135 RAIELLHRVGIKDhrdimaSYPNELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILL 214
Cdd:COG4604 118 EAIAYLDLEDLAD------RYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVI 191
|
90 100 110
....*....|....*....|....*....|....*.
gi 1403710885 215 TSNDIKSISEWCDQISVLYCGQNTESAPTEILIESP 250
Cdd:COG4604 192 VLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPE 227
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
138-218 |
1.89e-04 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 42.23 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 138 ELLHRVGIKD--HRDImasypNELTEGEGQKVMIAMAV-----ANQP--RLLIADEPTNALESTTALQVFRLLSSMNQnQ 208
Cdd:PRK03695 109 EVAEALGLDDklGRSV-----NQLSGGEWQRVRLAAVVlqvwpDINPagQLLLLDEPMNSLDVAQQAALDRLLSELCQ-Q 182
|
90
....*....|
gi 1403710885 209 GTTILLTSND 218
Cdd:PRK03695 183 GIAVVMSSHD 192
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
26-54 |
4.25e-04 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 42.09 E-value: 4.25e-04
10 20
....*....|....*....|....*....
gi 1403710885 26 VNLSLNEGEITGLVGESGSGKSLIAKVIC 54
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLT 379
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-233 |
4.60e-04 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 41.20 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 32 EGEITGLVGESGSGKSLIAKVICNAIKEN---------WIITADRFRfhdvellklsphkrrkivGKEISMIFQNPLS-C 101
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNlgkfddppdWDEILDEFR------------------GSELQNYFTKLLEgD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 102 LDPSRKigKQLIQNIPNwtfknkwwkwfgWKKRRAIELLHRV---GIKDH-------RDIMASYPNELTEGEGQKVMIAM 171
Cdd:cd03236 87 VKVIVK--PQYVDLIPK------------AVKGKVGELLKKKderGKLDElvdqlelRHVLDRNIDQLSGGELQRVAIAA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1403710885 172 AVANQPRLLIADEPTNALESTTALQVFRLLSSMNQnQGTTILLTSNDIKSISEWCDQISVLY 233
Cdd:cd03236 153 ALARDADFYFFDEPSSYLDIKQRLNAARLIRELAE-DDNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
155-232 |
5.34e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.94 E-value: 5.34e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1403710885 155 YPNELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSNDIKSISEwCDQISVL 232
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVF 1431
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
138-219 |
7.65e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 41.31 E-value: 7.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 138 ELLHRVGIKDhrdIMASYPNELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSN 217
Cdd:COG1245 438 EIIKPLGLEK---LLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDH 514
|
..
gi 1403710885 218 DI 219
Cdd:COG1245 515 DI 516
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
21-187 |
8.30e-04 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 41.20 E-value: 8.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 21 KIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICN---------AIKENWIITA---DRFRFHDVELLK--LSPHKRRKI 86
Cdd:COG0488 12 PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGelepdsgevSIPKGLRIGYlpqEPPLDDDLTVLDtvLDGDAELRA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 87 VGKEISMIFQNPLSCLDPSRKIGK--QLIQNIPNWTFknkwwkwfgwkKRRAIELLHRVGIKD---HRDImasypNELTE 161
Cdd:COG0488 92 LEAELEELEAKLAEPDEDLERLAElqEEFEALGGWEA-----------EARAEEILSGLGFPEedlDRPV-----SELSG 155
|
170 180
....*....|....*....|....*.
gi 1403710885 162 GEGQKVMIAMAVANQPRLLIADEPTN 187
Cdd:COG0488 156 GWRRRVALARALLSEPDLLLLDEPTN 181
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
165-244 |
9.23e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.87 E-value: 9.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 165 QKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMnQNQGTTILLTSNDIKSISEWCDQISVLYCGQNTESAPTE 244
Cdd:PRK10982 141 QMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLA 219
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
159-247 |
1.17e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 40.76 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 159 LTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQnQGTTILLTSNDIKSISEWCDQISVLYCGQ-- 236
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKA-EGLSIILVSSEMPEVLGMSDRILVMHEGRis 474
|
90
....*....|....
gi 1403710885 237 ---NTESAPTEILI 247
Cdd:PRK10762 475 gefTREQATQEKLM 488
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
162-236 |
1.30e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 40.86 E-value: 1.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1403710885 162 GEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLT----SNDiksISEWCDQISVLYCGQ 236
Cdd:TIGR00956 213 GERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAiyqcSQD---AYELFDKVIVLYEGY 288
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-97 |
1.50e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 40.21 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 1 MALLDICNLNieiQTSNGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVIC--NAIKENWIITADRfRFHDVEllkl 78
Cdd:PRK11650 1 MAGLKLQAVR---KSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAglERITSGEIWIGGR-VVNELE---- 72
|
90
....*....|....*....
gi 1403710885 79 sPHKRrkivgkEISMIFQN 97
Cdd:PRK11650 73 -PADR------DIAMVFQN 84
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
17-236 |
1.52e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 40.30 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 17 NGRIKIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIKENWiiTADRFrfhdvellklsphkrrkIVGKEISMifQ 96
Cdd:PRK13549 272 NPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRW--EGEIF-----------------IDGKPVKI--R 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 97 NPLS------CLDPS-RKigKQLI-------QNIpnwTFKNKWWKWFGWKKRRAIELLHRVGIKDHRDIMASYP----NE 158
Cdd:PRK13549 331 NPQQaiaqgiAMVPEdRK--RDGIvpvmgvgKNI---TLAALDRFTGGSRIDDAAELKTILESIQRLKVKTASPelaiAR 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1403710885 159 LTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQnQGTTILLTSNDIKSISEWCDQISVLYCGQ 236
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQ-QGVAIIVISSELPEVLGLSDRVLVMHEGK 482
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
33-224 |
2.57e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 37.74 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 33 GEITGLVGESGSGKSLIAKVICNAIKEnwiitadrfRFHDVELLKLSphkrrkivgkeismifqnplscldpsrkigkql 112
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGP---------PGGGVIYIDGE--------------------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 113 iqnipnwtfknkwwkwfgwkkrraiELLHRVGIKDHRDIMASYPNELTEGEGQKVMIAMAVANQPRLLIADEPTNALEST 192
Cdd:smart00382 40 -------------------------DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAE 94
|
170 180 190
....*....|....*....|....*....|....*..
gi 1403710885 193 T-----ALQVFRLLSSMNQNQGTTILLTSNDIKSISE 224
Cdd:smart00382 95 QealllLLEELRLLLLLKSEKNLTVILTTNDEKDLGP 131
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
138-230 |
3.73e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 39.02 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403710885 138 ELLHRVGIKDhrdIMASYPNELTEGEGQKVMIAMAVANQPRLLIADEPTNALESTTALQVFRLLSSMNQNQGTTILLTSN 217
Cdd:PRK13409 436 EIIKPLQLER---LLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDH 512
|
90
....*....|...
gi 1403710885 218 DIKSIsewcDQIS 230
Cdd:PRK13409 513 DIYMI----DYIS 521
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
21-58 |
4.20e-03 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 38.89 E-value: 4.20e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1403710885 21 KIVDGVNLSLNEGEITGLVGESGSGKSLIAKVICNAIK 58
Cdd:COG0488 329 TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELE 366
|
|
| |
